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Structural Determinants for Binding of Sorting Nexin 17 (SNX17) to the Cytoplasmic Adaptor Protein Krev Interaction Trapped 1 (KRIT1)
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LRP1 and integrins are known cargoes of SNX17.
“These proteins are primarily PM proteins and include six integrins and LRP1, which are known cargoes of SNX174,31,35,36.”
From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [31]
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Lee, J., Retamal, C., Cuitiño, L., Caruano-Yzermans, A., Shin, J.-E., van Kerkhof, P., Marzolo, M.-P., & Bu, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800642200 · Cited by 162
Sorting nexin 17 facilitates LRP recycling in the early endosome
van Kerkhof, P., Lee, J., McCormick, L., Tetrault, E., Lu, W., Schoenfish, M., Oorschot, V., Strous, G. J., Klumperman, J., & Bu, G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600756 · Cited by 148
Stockinger, W., Sailler, B., Strasser, V., Recheis, B., Fasching, D., Kahr, L., Schneider, W. J., & Nimpf, J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf435 · Cited by 130
Burden, J. J., Sun, X.-M., García, A. B. G., & Soutar, A. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313689200 · Cited by 82
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
Flagged first, then by citations
Research works printed but not linked: 48
- Carlton, 2005, Sorting nexins: unifying trends and new perspectives, Traffic, 6, 75, 10.1111/j.1600-0854.2005.00260.x · DOI
- Cullen, 2008, Endosomal sorting and signalling: an emerging role for sorting nexins, Nat. Rev. Mol. Cell Biol, 9, 574, 10.1038/nrm2427 · DOI · Paper page
- Florian, 2001, A new member of the sorting nexin family interacts with the C-terminus of P-selectin, Biochem. Biophys. Res. Commun, 281, 1045, 10.1006/bbrc.2001.4467 · DOI · Paper page
- Knauth, 2005, Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking, J. Mol. Biol, 347, 813, 10.1016/j.jmb.2005.02.004 · DOI · Paper page
- Böttcher, 2012, Sorting nexin 17 prevents lysosomal degradation of beta1 integrins by binding to the beta1-integrin tail, Nat. Cell Biol, 14, 584, 10.1038/ncb2501 · DOI · Paper page
- Steinberg, 2012, SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways, J. Cell Biol, 197, 219, 10.1083/jcb.201111121 · DOI · Paper page
- Adachi, 2010, Adaptor protein sorting nexin 17 interacts with the scavenger receptor FEEL-1/stabilin-1 and modulates its expression on the cell surface, Biochim. Biophys. acta, 1803, 553, 10.1016/j.bbamcr.2010.02.011 · DOI · Paper page
- Ghai, 2011, Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases, Proc. Natl. Acad. Sci. U.S.A, 108, 7763, 10.1073/pnas.1017110108 · DOI · Paper page
- Pearson, 2000, Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain, Cell, 101, 259, 10.1016/S0092-8674(00)80836-3 · DOI
- Chishti, 1998, The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane, Trends Biochem. Sci, 23, 281, 10.1016/S0968-0004(98)01237-7 · DOI · Paper page
- Bonifacino, 2003, Signals for sorting of transmembrane proteins to endosomes and lysosomes, Annu. Rev. Biochem, 72, 395, 10.1146/annurev.biochem.72.121801.161800 · DOI · Paper page
- Chen, 1990, NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor, J. Biol. Chem, 265, 3116, 10.1016/S0021-9258(19)39742-X · DOI · Paper page
- Uhlik, 2005, Structural and evolutionary division of phosphotyrosine binding (PTB) domains, J. Mol. Biol, 345, 1, 10.1016/j.jmb.2004.10.038 · DOI
- García-Alvarez, 2003, Structural determinants of integrin recognition by talin, Mol. Cell, 11, 49, 10.1016/S1097-2765(02)00823-7 · DOI
- Ghai, 2013, Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins, Proc. Natl. Acad. Sci. U.S.A, 110, E643, 10.1073/pnas.1216229110 · DOI · Paper page
- Seog, 2008, Sorting nexin 17 interacts directly with kinesin superfamily KIF1Bβ protein, Korean J. Physiol. Pharmacol, 12, 199, 10.4196/kjpp.2008.12.4.199 · DOI
- Wu, 2007, Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening, Proteomics, 7, 1775, 10.1002/pmic.200601006 · DOI
- Czubayko, 2006, Sorting nexin 17, a non-self-assembling and a PtdIns3P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1, Biochem. Biophys. Res. Commun, 345, 1264, 10.1016/j.bbrc.2006.04.129 · DOI · Paper page
- Yadla, 2010, Cerebral cavernous malformations as a disease of vascular permeability: from bench to bedside with caution, Neurosurg. Focus, 29, E4, 10.3171/2010.5.FOCUS10121 · DOI
- Laberge-le Couteulx, 1999, Truncating mutations in CCM1, encoding KRIT1, cause hereditary cavernous angiomas, Nat. Genet, 23, 189, 10.1038/13815 · DOI
- Fisher, 2014, Signaling pathways and the cerebral cavernous malformations proteins: lessons from structural biology, Cell Mol. Life Sci, 71, 1881, 10.1007/s00018-013-1532-9 · DOI
- Serebriiskii, 1997, Association of Krev-1/rap1a with Krit1, a novel ankyrin repeat-containing protein encoded by a gene mapping to 7q21–22, Oncogene, 15, 1043, 10.1038/sj.onc.1201268 · DOI
- Béraud-Dufour, 2007, Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1, FEBS J, 274, 5518, 10.1111/j.1742-4658.2007.06068.x · DOI
- Francalanci, 2009, Structural and functional differences between KRIT1A and KRIT1B isoforms: a framework for understanding CCM pathogenesis, Exp. Cell Res, 315, 285, 10.1016/j.yexcr.2008.10.006 · DOI
- Liu, 2013, Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation, Mol. Cell, 49, 719, 10.1016/j.molcel.2012.12.005 · DOI
- Zawistowski, 2005, CCM1 and CCM2 protein interactions in cell signaling: implications for cerebral cavernous malformations pathogenesis, Hum. Mol. Genet, 14, 2521, 10.1093/hmg/ddi256 · DOI
- Zhang, 2007, Interaction between krit1 and malcavernin: implications for the pathogenesis of cerebral cavernous malformations, Neurosurgery, 60, 353, 10.1227/01.NEU.0000249268.11074.83 · DOI
- Faurobert, 2010, Recent insights into cerebral cavernous malformations: a complex jigsaw puzzle under construction, FEBS J, 277, 1084, 10.1111/j.1742-4658.2009.07537.x · DOI
- Gingras, 2013, The structure of the ternary complex of Krev interaction trapped 1 (KRIT1) bound to both the Rap1 GTPase and the heart of glass (HEG1) cytoplasmic tail, J. Biol. Chem, 288, 23639, 10.1074/jbc.M113.462911 · DOI
- Kleaveland, 2009, Regulation of cardiovascular development and integrity by the heart of glass-cerebral cavernous malformation protein pathway, Nat. Med, 15, 169, 10.1038/nm.1918 · DOI
- Gingras, 2012, Structural basis of the junctional anchorage of the cerebral cavernous malformations complex, J. Cell Biol, 199, 39, 10.1083/jcb.201205109 · DOI
- Draheim, 2014, Cerebral cavernous malformation proteins at a glance, J. Cell Sci, 127, 701
- Luft, 1999, A method to produce microseed stock for use in the crystallization of biological macromolecules, Acta Crystallogr. D, 55, 988, 10.1107/S0907444999002085 · DOI
- Otwinowski, 1997, Processing of x-ray diffraction data collected in oscillation mode, Methods Enzymol, 276, 307, 10.1016/S0076-6879(97)76066-X · DOI · Paper page
- McCoy, 2007, Phaser crystallographic software, J. Appl. Crystallogr, 40, 658, 10.1107/S0021889807021206 · DOI · Paper page
- Emsley, 2004, Coot: model-building tools for molecular graphics, Acta Crystallogr. D Biol. Crystallogr, 60, 2126, 10.1107/S0907444904019158 · DOI · Paper page
- Adams, 2010, PHENIX: a comprehensive Python-based system for macromolecular structure solution, Acta Crystallogr. D Biol. Crystallogr, 66, 213, 10.1107/S0907444909052925 · DOI · Paper page
- Morin, 2013, Collaboration gets the most out of software, Elife, 2, e01456, 10.7554/eLife.01456 · DOI
- Zhang, 2001, Interaction between krit1 and icap1 α infers perturbation of integrin β1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation, Hum. Mol. Genet, 10, 2953, 10.1093/hmg/10.25.2953 · DOI
- Hamada, 2000, Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain, EMBO J, 19, 4449, 10.1093/emboj/19.17.4449 · DOI
- Holm, 2010, Dali server: conservation mapping in 3D, Nucleic Acids Res, 38, W545, 10.1093/nar/gkq366 · DOI · Paper page
- Landau, 2005, ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures, Nucleic Acids Res, 33, W299, 10.1093/nar/gki370 · DOI
- Bansal, 1991, The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation, Cell, 67, 1195, 10.1016/0092-8674(91)90295-A · DOI · Paper page
- Lawrence, 1993, Shape complementarity at protein-protein interfaces, J. Mol. Biol, 234, 946, 10.1006/jmbi.1993.1648 · DOI
- Li, 2012, Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1), J. Biol. Chem, 287, 22317, 10.1074/jbc.M112.361295 · DOI
- Farfán, 2013, A sorting nexin 17-binding domain within the LRP1 cytoplasmic tail mediates receptor recycling through the basolateral sorting endosome, Traffic, 14, 823, 10.1111/tra.12076 · DOI · Paper page
- Balana, 2013, Ras-association domain of sorting nexin 27 is critical for regulating expression of GIRK potassium channels, PLoS One, 8, e59800, 10.1371/journal.pone.0059800 · DOI
- Ghai, 2011, PX-FERM proteins: A link between endosomal trafficking and signaling?, Small GTPases, 2, 259, 10.4161/sgtp.2.5.17276 · DOI
Cited by
Sorted by citations
Structural basis for Retriever-SNX17 assembly and endosomal sorting
Singla, A., Boesch, D. J., Fung, H. Y. J., Ngoka, C., Enriquez, A. S., Song, R., Kramer, D. A., Han, Y., Banarer, E., Lemoff, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54583-6 · Cited by 23
SNX17 Mediates Dendritic Spine Maturation via p140Cap
Cui, Q., Liang, S., Li, H., Guo, Y., Lv, J., Wang, X., Qin, P., Xu, H., Huang, T. Y., Lu, Y., et al. (2024) · Molecular Neurobiology · doi:10.1007/s12035-023-03620-4 · Cited by 3
Metadata
- Authors
- Stiegler, A. L., Zhang, R., Liu, W., & Boggon, T. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-09
- Volume
- 289
- Issue
- 36
- Pages
- 25362-25373
- ISSN
- 0021-9258
- Cited by
- 32
- References
- 5
- Language
- en
- Licence
- Funders
- National Institutes of Health (R01 NS085078)
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