The emerging role of sorting nexins in cardiovascular diseases
Open accessAbstract
The sorting nexin (SNX) family consists of a diverse group of cytoplasmic- and membrane-associated phosphoinositide-binding proteins that play pivotal roles in the regulation of protein trafficking. This includes the entire endocytic pathway, such as endocytosis, endosomal sorting, and endosomal signaling. Dysfunctions of SNX pathway are involved in several forms of cardiovascular disease (CVD). Moreover, SNX gene variants are associated with CVDs. In this review, we discuss the current knowledge on SNX-mediated regulatory mechanisms and their roles in the pathogenesis and treatment of CVDs.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Impairment of SNX pathway is responsible for development of various forms of cardiovascular disease.
“Impairment of SNX pathway is responsible for the development of various forms of cardiovascular disease (CVD) [126].”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [126]
The Conclusions and perspectives table reports that SNX1 loss raises blood pressure, while the section on other cardiovascular diseases describes a mechanism by which SNX13 loss promotes heart failure. But the coronary artery disease section explicitly says direct evidence of a causal relationship is lacking. The claim overstates the evidence by treating SNX impairment as an established cause of various forms of CVD. (LLM, conf=0.90)
Experimental — accuracy not yet measuredSeveral endocytic proteins including SNX, epsins, and Dab2 play an indispensable role in cardiovascular diseases.
“Several endocytic proteins including sorting nexin (SNX), epsins, and disabled homolog 2 (Dab2) play an indispensable role in cardiovascular diseases [126].”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [126]
The Abstract and Conclusions and perspectives describe sorting nexins as endocytic-trafficking proteins with roles in cardiovascular disease. The supplied passages and searches for “epsins” and “Dab2” provide no support for attributing those proteins’ cardiovascular roles to this source. Page numbers were not available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredSNX19 is associated with coronary artery disease.
“Further, studies have also established the association of other SNX, such as SNX19, with coronary artery disease.”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [126]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Ding, M., Bhupathiraju, S. N., Satija, A., van Dam, R. M., & Hu, F. B. (2014) · Circulation · doi:10.1161/circulationaha.113.005925 · Cited by 565 · see citing works
Haft, C. R., de la Luz Sierra, M., Barr, V. A., Haft, D. H., & Taylor, S. I. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7278 · Cited by 244 · see citing works
Genetics and Genomics of Single-Gene Cardiovascular Diseases
Marian, A. J., van Rooij, E., & Roberts, R. (2016) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2016.09.968 · Cited by 48 · see citing works
Sorting nexin 17 regulates ApoER2 recycling and reelin signaling
Sotelo, P., Farfán, P., Benitez, M. L., Bu, G., & Marzolo, M.-P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093672 · Cited by 47 · see citing works
Flagged first, then by citations
Research works printed but not linked: 103
- [1]Benjamin E.J., Virani S.S., Callaway C.W., Chamberlain A.M., Chang A.R., Cheng S. (2018) Heart Disease and Stroke Statistics-2018 Update: A Report From the American Heart Association. Circulation 137, e67– e492 10.1161/CIR.0000000000000558 29386200 · DOI · Paper page
- [2]Dunbar S.B., Khavjou O.A., Bakas T., Hunt G., Kirch R.A., Leib A.R. (2015) Projected Costs of Informal Caregiving for Cardiovascular Disease: 2015 to 2035: A Policy Statement From the American Heart Association. Circulation 137, e558– e577 29632217
- [3]Wu Y., Benjamin E.J. and MacMahon S. (2016) Prevention and control of cardiovascular disease in the rapidly changing economy of China. Circulation 133, 2545– 2560 10.1161/CIRCULATIONAHA.115.008728 27297347 PMC4910645 · DOI
- [4]Sacks F.M., Lichtenstein A.H., Wu J.H.Y., Appel L.J., Creager M.A., Kris-Etherton P.M. (2017) Dietary fats and cardiovascular disease: a presidential advisory from the American Heart Association. Circulation 136, e1– e23 10.1161/CIR.0000000000000510 28620111 · DOI · Paper page
- [6]Erqou S., Clougherty J.E., Olafiranye O., Magnani J.W., Aiyer A., Tripathy S. (2018) Particulate matter air pollution and racial differences in cardiovascular disease risk. Arterioscler. Thromb. Vasc. Biol. 38, 935– 942 10.1161/ATVBAHA.117.310305 29545240 PMC5864550 · DOI
- [7]Lu X., Ye Z., Zheng S., Ren H., Zeng J., Wang X. (2018) Long-term exposure of fine particulate matter causes hypertension by impaired renal D1 receptor-mediated sodium excretion via upregulation of G-protein-coupled receptor kinase type 4 expression in Sprague-Dawley rats. J. Am. Heart Assoc. 7, pii: e007185 10.1161/JAHA.117.007185 PMC5778966 29307864 · DOI
- [8]Arnett D.K., Baird A.E., Barkley R.A., Basson C.T., Boerwinkle E., Ganesh S.K. (2007) Relevance of genetics and genomics for prevention and treatment of cardiovascular disease: a scientific statement from the American Heart Association Council on Epidemiology and Prevention, the Stroke Council, and the Functional Genomics and Translational Biology Interdisciplinary Working Group. Circulation 115, 2878– 2901 10.1161/CIRCULATIONAHA.107.183679 17515457 · DOI
- [9]Ashley E.A., Hershberger R.E., Caleshu C., Ellinor P.T., Garcia J.G., Herrington D.M. (2012) Genetics and cardiovascular disease: a policy statement from the American Heart Association. Circulation 126, 142– 157 10.1161/CIR.0b013e31825b07f8 22645291 PMC3721666 · DOI
- [10]Bauersachs J. and Heymans S. (2018) Scientific updates on the interaction of genes, epigenetics, and multicellularity in cardiovascular diseases: the Working Group of Myocardial Function of the ESC. Cardiovasc. Res. 114, 1271– 1272 10.1093/cvr/cvy149 29992298 · DOI
- [12]Gallon M. and Cullen P.J. (2015) Retromer and sorting nexins in endosomal sorting. Biochem. Soc. Trans. 43, 33– 47 10.1042/BST20140290 25619244 · DOI
- [13]Cullen P.J. (2008) Endosomal sorting and signalling: an emerging role for sorting nexins. Nat. Rev. Mol. Cell Biol. 9, 574– 582 10.1038/nrm2427 18523436 · DOI
- [14]Liu J.J. (2016) Retromer-mediated protein sorting and vesicular trafficking. J. Genet. Genomics 43, 165– 177 10.1016/j.jgg.2016.02.006 27157806 · DOI
- [15]Teasdale R.D. and Collins B.M. (2012) Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease. Biochem. J. 441, 39– 59 10.1042/BJ20111226 22168438 · DOI
- [16]Chandra M. and Collins B.M. (2018) The Phox Homology (PX) Domain. Adv. Exp. Med. Biol., in press 2018 Mar 23. [Epub ahead of print] 10.1007/5584_2018_185 29569114 · DOI
- [17]Zhang H., Huang T., Hong Y., Yang W., Zhang X., Luo H. (2018) The retromer complex and sorting nexins in neurodegenerative diseases. Front. Aging Neurosci. 10, 79 10.3389/fnagi.2018.00079 29632483 PMC5879135 · DOI
- [18]van Weering J.R., Verkade P. and Cullen P.J. (2017) SNX-BAR proteins in phosphoinositide-mediated, tubular-based endosomal sorting. Semin. Cell Dev. Biol. 21, 371– 380 10.1016/j.semcdb.2009.11.009 PMC4052211 19914387 · DOI
- [19]Lauffer B.E., Melero C., Temkin P., Lei C., Hong W., Kortemme T. (2010) SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane. J. Cell Biol. 190, 565– 574 10.1083/jcb.201004060 20733053 PMC2928020 · DOI
- [20]Elwell C. and Engel J. (2018) Emerging role of retromer in modulating pathogen growth. Trends Microbiol. 26, 769– 780 10.1016/j.tim.2018.04.001 29703496 PMC6097928 · DOI
- [21]McNally K.E and Cullen P.J. (2018) Endosomal retrieval of cargo: retromer is not alone. Trends Cell Biol 28, 807– 822 10.1016/j.tcb.2018.06.005 30072228 · DOI
- [22]Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J., Heesom K.J. (2013) A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport. Nat. Cell Biol. 15, 461– 471 10.1038/ncb2721 23563491 PMC4052425 · DOI
- [23]Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y. (2013) Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down’s syndrome. Nat. Med. 19, 473– 480 10.1038/nm.3117 23524343 PMC3911880 · DOI
- [24]Harterink M., Port F., Lorenowicz M.J., McGough I.J., Silhankova M., Betist M.C. (2011) A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion. Nat. Cell Biol. 13, 914– 923 10.1038/ncb2281 21725319 PMC4052212 · DOI
- [25]Wassmer T., Attar N., Bujny M.V., Oakley J., Traer C.J. and Cullen P.J. (2007) A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J. Cell Sci. 120, 45– 54 10.1242/jcs.03302 17148574 · DOI
- [26]Singh V., Yang J., Yin J., Cole R., Tse M., Berman D.E. (2018) Cholera toxin inhibits SNX27-retromer-mediated delivery of cargo proteins to the plasma membrane. J. Cell Sci. 131, pii: jcs218610 10.1242/jcs.218610 PMC6127729 30030371 · DOI
- [27]Kvainickas A., Jimenez-Orgaz A., Nägele H., Hu Z., Dengjel J. and Steinberg F. (2017) Cargo-selective SNX-BAR proteins mediate retromer trimer independent retrograde transport. J. Cell Biol. 216, 3677– 3693 10.1083/jcb.201702137 28935632 PMC5674888 · DOI
- [28]Harterink M., Port F., Lorenowicz M.J., McGough I.J., Silhankova M., Betist M.C. (2011) A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion. Nat. Cell Biol. 13, 914– 923 10.1038/ncb2281 21725319 PMC4052212 · DOI
- [29]Lee S., Chang J. and Blackstone C. (2016) FAM21 directs SNX27-retromer cargoes to the plasma membrane by preventing transport to the Golgi apparatus. Nat. Commun. 7, 10939 10.1038/ncomms10939 26956659 PMC4786876 · DOI
- [30]Soulet F., Yarar D., Leonard M. and Schmid S.L. (2005) SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis. Mol. Biol. Cell 16, 2058– 2067 10.1091/mbc.e04-11-1016 15703209 PMC1073683 · DOI
- [31]Bendris N. and Schmid S.L. (2017) Endocytosis, metastasis and beyond: multiple facets of SNX9. Trends Cell Biol. 27, 189– 200 10.1016/j.tcb.2016.11.001 27989654 PMC5318277 · DOI
- [32]Park J., Kim Y., Lee S., Park J.J., Park Z.Y., Sun W. (2010) SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane. J. Cell Sci. 123, 1742– 1750 10.1242/jcs.064170 20427313 · DOI
- [33]Villar V.A., Armando I., Sanada H., Frazer L.C., Russo C.M., Notario P.M. (2013) Novel role of sorting nexin 5 in renal D(1) dopamine receptor trafficking and function: implications for hypertension. FASEB J. 27, 1808– 1819 10.1096/fj.12-208439 23195037 PMC3633819 · DOI · Paper page
- [34]Villar V.A., Jones J.E., Armando I., Asico L.D., Escano C.S. Jr., Lee H. (2013) Sorting nexin 1 loss results in D5 dopamine receptor dysfunction in human renal proximal tubule cells and hypertension in mice. J. Biol. Chem. 288, 152– 163 10.1074/jbc.M112.428458 23152498 PMC3537009 · DOI · Paper page
- [35]Li C., Ma W., Yin S., Liang X., Shu X., Pei D. (2016) Sorting Nexin 11 Regulates Lysosomal Degradation of Plasma Membrane TRPV3. Traffic 17, 500– 514 10.1111/tra.12379 26818531 · DOI
- [36]Kurten R.C., Cadena D.L. and Gill G.N. (1996) Enhanced degradation of EGF receptors by a sorting nexin, SNX1. Science 272, 1008– 1010 10.1126/science.272.5264.1008 8638121 · DOI
- [37]Fuster J.J., González J.M., Edo M.D., Viana R., Boya P., Cervera J., Tumor suppressor p27(Kip1) undergoes endolysosomal degradation through its interaction with sorting nexin 6. FASEB J. 24, 2998– 3009 10.1096/fj.09-138255 20228253 · DOI
- [38]Böttcher R.T., Stremmel C., Meves A., Meyer H., Widmaier M., Tseng H.Y. (2012) Sorting nexin 17 prevents lysosomal degradation of β1 integrins by binding to the β1-integrin tail. Nat. Cell Biol. 14, 584– 592 10.1038/ncb2501 22561348 · DOI · Paper page
- [39]Williams R., Schlüter T., Roberts M.S., Knauth P., Bohnensack R. and Cutler D.F. (2004) Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin. Mol. Biol. Cell. 15, 3095– 3105 10.1091/mbc.e04-02-0143 15121882 PMC452567 · DOI · Paper page
- [40]Kim N.Y., Cho M.H., Won S.H., Kang H.J., Yoon S.Y. and Kim D.H. (2017) Sorting nexin-4 regulates β-amyloid production by modulating β-site-activating cleavage enzyme-1. Alzheimers Res. Ther. 9, 4 10.1186/s13195-016-0232-8 28109317 PMC5251330 · DOI
- [41]Bareja A., Hodgkinson C.P., Soderblom E., Waitt G. and Dzau V.J. (2018) The proximity-labeling technique BioID identifies sorting nexin 6 as a member of the insulin-like growth factor 1 (IGF1)-IGF1 receptor pathway. J. Biol. Chem. 293, 6449– 6459 10.1074/jbc.RA118.002406 29530981 PMC5925803 · DOI
- [42]Le Y., Zhang S., Ni J., You Y., Luo K., Yu Y. (2018) Sorting nexin 10 controls mTOR activation through regulating amino-acid metabolism in colorectal cancer. Cell Death Dis 9, 666 10.1038/s41419-018-0719-2 29867114 PMC5986761 · DOI
- [43]Wilkes M.C., Repellin C.E., Kang J.H., Andrianifahanana M., Yin X. and Leof E.B. (2015) Sorting nexin 9 differentiates ligand-activated Smad3 from Smad2 for nuclear import and transforming growth factor β signaling. Mol. Biol. Cell 26, 3879– 3891 10.1091/mbc.E15-07-0545 26337383 PMC4626071 · DOI
- [44]Li F., Yang J., Jones J.E., Villar V.A., Yu P., Armando I. (2015) Sorting nexin 5 and dopamine d1 receptor regulate the expression of the insulin receptor in human renal proximal tubule cells. Endocrinology 156, 2211– 2221 10.1210/en.2014-1638 25825816 PMC4430625 · DOI
- [45]Aboghe D.H., Yoshioka M., Phaneuf D. and St-Amand J. (2009) Regulation of gene expression by estrogen in mammary gland of wild type and estrogen receptor alpha knockout mice. J. Steroid Biochem. Mol. Biol. 113, 116– 126 10.1016/j.jsbmb.2008.12.002 19126430 · DOI
- [46]Muirhead G. and Dev K.K. (2014) The expression of neuronal sorting nexin 8 (SNX8) exacerbates abnormal cholesterol levels. J. Mol. Neurosci. 53, 125– 134 10.1007/s12031-013-0209-z 24362679 · DOI
- [47]Baumann C., Lindholm C.K., Rimoldi D. and Lévy F. (2010) The E3 ubiquitin ligase Itch regulates sorting nexin 9 through an unconventional substrate recognition domain. FEBS J 277, 2803– 2814 10.1111/j.1742-4658.2010.07698.x 20491914 · DOI
- [48]Duclos C.M., Champagne A., Carrier J.C., Saucier C., Lavoie C.L. and Denault J.B. (2017) Caspase-mediated proteolysis of the sorting nexin 2 disrupts retromer assembly and potentiates Met/hepatocyte growth factor receptor signaling. Cell Death Discov. 3, 16100 10.1038/cddiscovery.2016.100 28179995 PMC5253419 · DOI
- [49]Wassmer T., Attar N., Bujny M.V., Oakley J., Traer C.J. and Cullen P.J. (2017) A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J. Cell Sci. 120, 45– 54 10.1242/jcs.03302 17148574 · DOI
- [50]MaCaulay S.L., Stoichevska V., Grusovin J., Gough K.H., Castelli L.A. and Ward C.W. (2003) Insulin stimulates movement of sorting nexin 9 between cellular compartments: a putative role mediating cell surface receptor expression and insulin action. Biochem. J. 376, 123– 134 10.1042/bj20030130 12917015 PMC1223752 · DOI
- [51]Yang Z., Hong L.K., Follett J., Wabitsch M., Hamilton N.A., Collins B.M. (2016) Functional characterization of retromer in GLUT4 storage vesicle formation and adipocyte differentiation. FASEB J. 30, 1037– 1050 10.1096/fj.15-274704 26581601 · DOI
- [52]Zhang M.Z. and Harris R.C. (2015) Antihypertensive mechanisms of intra-renal dopamine. Curr. Opin. Nephrol. Hypertens. 24, 117– 122 10.1097/MNH.0000000000000104 25594544 PMC4651846 · DOI
- [53]Yang J., Villar V.A., Jones J.E., Jose P.A. and Zeng C. (2015) G protein-coupled receptor kinase 4: role in hypertension. Hypertension 65, 1148– 1155 10.1161/HYPERTENSIONAHA.115.05189 25870190 PMC6350509 · DOI
- [54]Guo Y. and Jose P.A. (2011) C-terminal di-leucine motif of dopamine D receptor plays an important role in its plasma membrane trafficking. PLoS One 6, e29204 10.1371/journal.pone.0029204 22206002 PMC3242775 · DOI
- [55]Li F., Yang J., Villar V.A.M., Asico L.D., Ma X., Armando I. (2018) Loss of renal SNX5 results in impaired IDE activity and insulin resistance in mice. Diabetologia 61, 727– 737 10.1007/s00125-017-4482-1 29080975 PMC6342204 · DOI · Paper page
- [58]Carey R.M., Schoeffel C.D., Gildea J.J., Jones J.E., McGrath H.E., Gordon L.N. (2012) Salt sensitivity of blood pressure is associated with polymorphisms in the sodium-bicarbonate cotransporter. Hypertension 60, 1359– 1366 10.1161/HYPERTENSIONAHA.112.196071 22987918 PMC3495588 · DOI
- [59]Heydorn A., Søndergaard B.P., Hadrup N., Holst B., Haft C.R. and Schwartz T.W. (2004) Distinct in vitro interaction pattern of dopamine receptor subtypes with adaptor proteins involved in post-endocytotic receptor targeting. FEBS Lett. 556, 276– 280 10.1016/S0014-5793(03)01431-5 14706863 · DOI
- [60]Vargas G.A. and Von Zastrow M. (2004) Identification of a novel endocytic recycling signal in the D1 dopamine receptor. J. Biol. Chem. 279, 37461– 37469 10.1074/jbc.M401034200 15192107 · DOI
- [61]Lamey M., Thompson M., Varghese G., Chi H., Sawzdargo M., George S.R. (2002) Distinct residues in the carboxyl tail mediate agonist-induced desensitization and internalization of the human dopamine D1 receptor. J. Biol. Chem. 277, 9415– 9421 10.1074/jbc.M111811200 11773080 · DOI
- [62]Jackson A., Iwasiow R.M., Chaar Z.Y., Nantel M.F. and Tiberi M. (2002) Homologous regulation of the heptahelical D1A receptor responsiveness: specific cytoplasmic tail regions mediate dopamine-induced phosphorylation, desensitization and endocytosis. J. Neurochem. 82, 683– 697 10.1046/j.1471-4159.2002.01001.x 12153492 · DOI
- [65]Rao F., Wessel J., Wen G., Zhang L., Rana B.K., Kennedy B.P. (2007) Renal albumin excretion: twin studies identify influences of heredity, environment, and adrenergic pathway polymorphism. Hypertension 49, 1015– 1031 10.1161/HYPERTENSIONAHA.106.081679 17353515 · DOI
- [66]Singh V., Yang J., Cha B., Chen T.E., Sarker R., Yin J. (2015) Sorting nexin 27 regulates basal and stimulated brush border trafficking of NHE3. Mol. Biol. Cell 26, 2030– 2043 10.1091/mbc.E14-12-1597 25851603 PMC4472014 · DOI
- [67]Boulkroun S., Ruffieux-Daidié D., Vitagliano J.J., Poirot O., Charles R.P., Lagnaz D. (2008) Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3. Am. J. Physiol. Renal Physiol. 295, F889– F900 10.1152/ajprenal.00001.2008 18632802 · DOI
- [68]Zhang Y., Lee E.T., Howard B.V., Best L.G., Umans J.G., Yeh J. (2013) Insulin resistance, incident cardiovascular diseases, and decreased kidney function among nondiabetic American Indians: the Strong Heart Study. Diabetes Care 36, 3195– 3200 10.2337/dc12-2368 23735722 PMC3781520 · DOI
- [69]Manucha W., Ritchie B. and Ferder L. (2015) Hypertension and insulin resistance: implications of mitochondrial dysfunction. Curr. Hypertens. Rep. 17, 504 10.1007/s11906-014-0504-2 25432896 · DOI
- [70]Harashima S., Horiuchi T., Wang Y., Notkins A.L., Seino Y. and Inagaki N. (2012) Sorting nexin 19 regulates the number of dense core vesicles in pancreatic β-cells. J. Diabetes Investig. 3, 52– 61 10.1111/j.2040-1124.2011.00138.x 24843546 PMC4014933 · DOI
- [71]Valera Mora M.E., Scarfone A., Calvani M., Greco A.V. and Mingrone G. (2003) Insulin clearance in obesity. J. Am. Coll. Nutr. 22, 487– 493 10.1080/07315724.2003.10719326 14684753 · DOI
- [72]Hjelle J.T., Oparil S. and Peterson D.R. (1984) Subcellular sites of insulin hydrolysis in renal proximal tubules. Am. J. Physiol. 246, F409– F416 6372510
- [73]Tang W.J. (2016) Targeting insulin-degrading enzyme to treat type 2 diabetes mellitus. Trends Endocrinol. Metab. 27, 24– 34 10.1016/j.tem.2015.11.003 26651592 PMC4698235 · DOI
- [74]Ghai R., Bugarcic A., Liu H., Norwood S.J., Skeldal S., Coulson E.J. (2013) Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. Proc. Natl. Acad. Sci U.S.A. 110, E643– F652 10.1073/pnas.1216229110 23382219 PMC3581954 · DOI · Paper page
- [76]Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J., Heesom K.J. (2013) A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport. Nat. Cell Biol. 15, 461– 471 10.1038/ncb2721 23563491 PMC4052425 · DOI
- [77]Chai W., Zhang X., Barrett E.J. and Liu Z. (2014) Glucagon-like peptide 1 recruits muscle microvasculature and improves insulin’s metabolic action in the presence of insulin resistance. Diabetes 63, 2788– 2799 10.2337/db13-1597 24658303 PMC4113068 · DOI · Paper page
- [78]Buenaventura T., Kanda N., Douzenis P.C., Jones B., Bloom S.R., Chabosseau P. (2018) A targeted RNAi screen identifies endocytic trafficking factors that control GLP-1 receptor signaling in pancreatic β-cells. Diabetes 67, 385– 399 10.2337/db17-0639 29284659 · DOI
- [79]Morrison A.C., Bare L.A., Chambless L.E., Ellis S.G., Malloy M., Kane J.P. (2007) Prediction of coronary heart disease risk using a genetic risk score: the Atherosclerosis Risk in Communities Study. Am. J. Epidemiol. 166, 28– 35 10.1093/aje/kwm060 17443022 · DOI
- [80]Bare L.A., Morrison A.C., Rowland C.M., Shiffman D., Luke M.M., Iakoubova O.A. (2007) Five common gene variants identify elevated genetic risk for coronary heart disease. Genet. Med. 9, 682– 689 10.1097/GIM.0b013e318156fb62 18073581 · DOI
- [81]Jeon H and Blacklow S.C. (2005) Structure and physiologic function of the low-density lipoprotein receptor. Annu. Rev. Biochem. 74, 535– 562 10.1146/annurev.biochem.74.082803.133354 15952897 · DOI
- [82]Burden J.J., Sun X.M., García A.B. and Soutar A.K. (2004) Sorting motifs in the intracellular domain of the low density lipoprotein receptor interact with a novel domain of sorting nexin-17. J. Biol. Chem. 279, 16237– 16245 10.1074/jbc.M313689200 14739284 · DOI · Paper page
- [83]van Kerkhof P., Lee J., McCormick L., Tetrault E., Lu W., Schoenfish M. (2005) Sorting nexin 17 facilitates LRP recycling in the early endosome. EMBO J 24, 285128– 285161 10.1038/sj.emboj.7600756 PMC1187941 16052210 · DOI · Paper page
- [84]Donoso M., Cancino J., Lee J., van Kerkhof P., Retamal C., Bu G. (2009) Polarized traffic of LRP1 involves AP1B and SNX17 operating on Y-dependent sorting motifs in different pathways. Mol. Biol. Cell 20, 481– 497 10.1091/mbc.e08-08-0805 19005208 PMC2613102 · DOI · Paper page
- [85]Farfán P., Lee J., Larios J., Sotelo P., Bu G. and Marzolo M.P. (2013) A sorting nexin 17-binding domain within the LRP1 cytoplasmic tail mediates receptor recycling through the basolateral sorting endosome. Traffic 14, 823– 838 10.1111/tra.12076 23593972 PMC3679278 · DOI · Paper page
- [87]Gullapalli A., Wolfe B.L., Griffin C.T., Magnuson T. and Trejo J. (2006) An essential role for SNX1 in lysosomal sorting of protease-activated receptor-1: evidence for retromer-, Hrs-, and Tsg101-independent functions of sorting nexins. Mol. Biol. Cell 17, 1228– 1238 10.1091/mbc.e05-09-0899 16407403 PMC1382312 · DOI
- [88]Raghavan S., Singh N.K., Mani A.M. and Rao G.N. (2018) Protease-activated receptor 1 inhibits cholesterol efflux and promotes atherogenesis via cullin 3-mediated degradation of the ABCA1 transporter. J. Biol. Chem. 293, 10574– 10589 10.1074/jbc.RA118.003491 29777060 PMC6036195 · DOI
- [89]Lin Y.J., Chang J.S., Liu X., Lin T.H., Huang S.M., Liao C.C. (2013) Sorting nexin 24 genetic variation associates with coronary artery aneurysm severity in Kawasaki disease patients. Cell Biosci 3, 44 10.1186/2045-3701-3-44 24268062 PMC4176999 · DOI
- [90]Florian V., Schlüter T. and Bohnensack R. (2001) A new member of the sorting nexin family interacts with the C-terminus of P-selectin. Biochem. Biophys. Res Commun. 281, 1045– 1050 10.1006/bbrc.2001.4467 11237770 · DOI · Paper page
- [91]Williams R., Schlüter T., Roberts M.S., Knauth P., Bohnensack R. and Cutler D.F. (2004) Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin. Mol. Biol. Cell 15, 3095– 3105 10.1091/mbc.e04-02-0143 15121882 PMC452567 · DOI · Paper page
- [92]Zhao D., Li X., Liang H., Zheng N., Pan Z., Zhou Y. (2018) SNX17 produces anti-arrhythmic effects by preserving functional SERCA2a protein in myocardial infarction. Int. J. Cardiol. 272, 298– 305 10.1016/j.ijcard.2018.07.025 30025651 · DOI
- [93]Li J., Li C., Zhang D., Shi D., Qi M., Feng J. (2014) SNX13 reduction mediates heart failure through degradative sorting of apoptosis repressor with caspase recruitment domain. Nat. Commun. 5, 5177 10.1038/ncomms6177 25295779 · DOI · Paper page
- [94]Bian Z., Feng Y., Xue Y., Hu Y., Wang Q., Zhou L. (2016) Down-regulation of SNX1 predicts poor prognosis and contributes to drug resistance in colorectal cancer. Tumor Biol. 37, 6619– 6625 10.1007/s13277-015-3814-3 26643894 · DOI
- [95]Ogi S., Fujita H., Kashihara M., Yamamoto C., Sonoda K., Okamoto I. (2013) Sorting nexin 2-mediated membrane trafficking of c-Met contributes to sensitivity of molecular-targeted drugs. Cancer Sci. 104, 573– 583 10.1111/cas.12117 23360489 PMC7657160 · DOI
- [96]Kokubo Y. and Iwashima Y. (2015) Higher blood pressure as a risk factor for diseases other than stroke and ischemic heart disease. Hypertension 66, 254– 259 10.1161/HYPERTENSIONAHA.115.03480 26077565 · DOI
- [97]Qi W.X., Fu S., Zhang Q. and Guo X.M. (2016) Incidence and risk of hypertension associated with ramucirumab in cancer patients: A systematic review and meta-analysis. J. Cancer Res. Ther. 12, 775– 781 10.4103/0973-1482.148700 27461650 · DOI
- [98]Nakagawa T. and Asahi M. (2013) β1-adrenergic receptor recycles via a membranous organelle, recycling endosome, by binding with sorting nexin27. J. Membr. Biol. 246, 571– 579 10.1007/s00232-013-9571-6 23780416 PMC3695668 · DOI
- [99]Shahin M.H., Conrado D.J., Gonzalez D., Gong Y., Lobmeyer M.T., Beitelshees A.L. (2018) Genome-Wide association approach identified novel genetic predictors of heart rate response to β-blockers. J. Am. Heart Assoc. 7, pii: e006463 10.1161/JAHA.117.006463 PMC5866313 29478026 · DOI
- [100]Lauffer B.E., Melero C., Temkin P., Lei C., Hong W., Kortemme T. (2010) SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane. J. Cell Biol. 190, 565– 574 10.1083/jcb.201004060 20733053 PMC2928020 · DOI
- [101]Temkin P., Lauffer B., Jäger S., Cimermancic P., Krogan N.J. and von Zastrow M. (2011) SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors. Nat. Cell Biol. 13, 715– 721 10.1038/ncb2252 21602791 PMC3113693 · DOI
- [102]Nooh M.M., Mancarella S. and Bahouth S.W. (2016) Identification of novel transplantable GPCR recycling motif for drug discovery. Biochem. Pharmacol. 120, 22– 32 10.1016/j.bcp.2016.09.011 27645110 PMC5079812 · DOI
- [103]Ma M.P. and Chircop M. (2012) SNX9, SNX18 and SNX33 are required for progression through and completion of mitosis. J. Cell Sci. 125, 4372– 4382 10.1242/jcs.105981 22718350 · DOI
- [104]Hanson B.J. and Hong W. (2003) Evidence for a role of SNX16 in regulating traffic between the early and later endosomal compartments. J. Biol. Chem. 278, 34617– 34630 10.1074/jbc.M300143200 12813048 · DOI
- [105]Brankatschk B., Pons V., Parton R.G. and Gruenberg J. (2011) Role of SNX16 in the dynamics of tubulo-cisternal membrane domains of late endosomes. PLoS One 6, e21771 10.1371/journal.pone.0021771 21754999 PMC3130770 · DOI
- [106]Vieira N., Deng F.M., Liang F.X., Liao Y., Chang J., Zhou G. (2014) SNX31: a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. PLoS One 9, e99644 10.1371/journal.pone.0099644 24914955 PMC4051706 · DOI
- [107]Ha C.M., Park D., Kim Y., Na M., Panda S., Won S. (2015) SNX14 is a bifunctional negative regulator for neuronal 5-HT6 receptor signaling. J. Cell Sci. 128, 1848– 1861 10.1242/jcs.169581 25795301 PMC6518326 · DOI
- [108]Hao X., Wang Y., Ren F., Zhu S., Ren Y., Jia B. (2011) SNX25 regulates TGF-β signaling by enhancing the receptor degradation. Cell Signal. 23, 935– 946 10.1016/j.cellsig.2011.01.022 21266196 · DOI
- [109]Feng T., Niu M., Ji C., Gao Y., Wen J., Bu G. (2016) SNX15 regulates cell surface recycling of APP and Aβ generation. Mol. Neurobiol. 53, 3690– 3701 10.1007/s12035-015-9306-z 26115702 PMC4691577 · DOI
- [110]Danson C., Brown E., Hemmings O.J., McGough I.J., Yarwood S., Heesom K.J. (2013) SNX15 links clathrin endocytosis to the PtdIns3P early endosome independently of the APPL1 endosome. J. Cell Sci. 126, 4885– 4899 10.1242/jcs.125732 23986476 PMC3820240 · DOI
- [111]Hoepfner S., Severin F., Cabezas A., Habermann B., Runge A., Gillooly D. (2005) Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B. Cell 121, 437– 450 10.1016/j.cell.2005.02.017 15882625 · DOI
Cited by
Sorted by citations
Insights of Endocytosis Signaling in Health and Disease
Pathak, C., Vaidya, F. U., Waghela, B. N., Jaiswara, P. K., Gupta, V. K., Kumar, A., Rajendran, B. K., & Ranjan, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032971 · Cited by 59 · see citing works
- Authors
- Yang, J., Villar, V. A. M., Rozyyev, S., Jose, P. A., & Zeng, C.
- Affiliations
- Army Medical University (CN)
- George Washington University (US)
- Division of Renal Diseases and Hypertension, Department of Medicine, and Department of Pharmacology/Physiology, The George Washington University School of Medicine and Health Sciences, Washington, DC 20052, U.S.A.
- Corresponding author
- Yang, Jian
- Zeng, Chunyu
- Venue
- Clinical Science
- Publisher
- Portland Press Ltd.
- Published
- 2019-03
- Volume
- 133
- Issue
- 5
- Pages
- 723-737
- ISSN
- 0143-5221 (ISSN-L)
- 1470-8736
- PMC
- PMC6418407
- OpenAlex
- W2921179399
- Cited by
- 55
- References
- 4
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 7 · 2023: 13 · 2022: 7 · 2021: 11 · 2020: 10
- FWCI
- 0.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Clinical Science (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81770425, 2018YFC1312700, 81570379, 81721001)
- National Institutes of Health (and 5P01HL074940)
- National Heart, Lung, and Blood Institute (P01HL074940, R01HL092196)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK039308)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- sorting nexins, phosphoinositide-binding proteins, protein trafficking, endocytosis, endosomal sorting, endosomal signaling, cardiovascular disease, pathogenesis, cardiovascular disease treatment
- MeSH terms
- Animals, Cardiovascular Diseases, Cardiovascular System, Endocytosis, Humans, Prognosis, Endosomes, Signal Transduction, Protein Transport, Sorting Nexins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review