A pleckstrin homology‐related domain in SHIP1 mediates membrane localization during Fcγ receptor‐induced phagocytosis
Abstract
SH2 domain-containing inositol-5'-phosphatase-1 (SHIP1) inhibits inflammation by hydrolyzing phosphoinositide-3'-kinase generated membrane phosphatidylinositol-3,4,5-trisphosphate (PIP(3)). Bioinformatic analysis of SHIP1 from multiple species revealed a pleckstrin homololgy-related (PH-R) domain, which we hypothesize mediates SHIP1's association with the membrane, a requirement for its biological function. Recombinant murine SHIP1 PH-R domain was subjected to biophysical and biochemical analysis. Residues K370 and K397 were found to be important for PH-R domain association with membrane PIP(3). Wild-type PH-R domain bound PIP(3) with 1.9 ± 0.2 nM affinity, while the affinity of a K370A/K397A substituted mutant was too low to measure. Wild-type (but not the K370A/K397A substituted) full-length SHIP1 protein, reconstitutes normal inhibition of Fcγ receptor-mediated phagocytosis when introduced into SHIP1(-/-) murine macrophages, reducing the number of phagocytic events by 2-fold as compared to SHIP1(-/-) cells. In fact, the PH-R-mediated membrane interaction appears to be a major mechanism by which SHIP1 is recruited to the membrane, since the K370A/K397A substitution reduced the recruitment of both full-length SHIP1 and the PH-R domain by ≥2-fold. We have previously shown that SHIP1 enzyme activity can be targeted for therapeutic purposes. The current studies suggest that molecules targeting the PH-R domain can also modulate SHIP1 function.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
SHIP1 deficiency has been associated with increased phagocytosis of various substrates in other models.
“However, SHIP1 deficiency has been associated with increased phagocytosis of various substrates in other models73,74.”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [74]
SH2 domain of SHIP1 can dock onto phosphorylated tyrosine residues to regulate the activity of receptors containing ITAMs/ITIMs.
“SH2 domain can dock onto phosphorylated tyrosine residues to regulate the activity of receptors containing immunoreceptor tyrosine activating/inhibiting motif (ITAMs/ITIMs).”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [106]
SHIP1 consists of an SH2 domain near its N-terminus that docks onto phosphorylated tyrosine residues, followed by a PH-L domain that binds PI(3,4,5)P3 and localizes SHIP1 to the membrane.
“SHIP1 consists of a Src homology 2 (SH2) domain near its N-terminus, which docks onto phosphorylated tyrosine residues, followed by a plectrin homology-like (PH-L) domain that binds to PI(3,4,5)P3 and localizes SHIP1 to the membrane [106].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [106]
SHIP1 binds to PI(3,4,5)P3 via its PH-L domain and dephosphorylates PI(3,4,5)P3 via its 5' phosphatase catalytic domain to generate PI(4,5)P2.
“SHIP1 binds to PI(3,4,5)P3 via its PH-L domain and dephosphorylates PI(3,4,5)P3 via its 5’ phosphatase catalytic domain to generate PI(4,5)P2.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [106]
SH2 domain is important for SHIP1's localization within the cell.
“This domain is also important for SHIP1’s localization within the cell.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [106]
SHIP1 negatively regulates microglia and macrophage phagocytosis, likely through its proposed regulation of TREM2, TLR4, FCγR and CR3-mediated signaling, and potentially other signaling pathways.
“Multiple studies support the hypothesis that SHIP1 negatively regulates microglia and macrophage phagocytosis, likely through its proposed regulation of TREM2 and TLR4, as well as Fc gamma receptor (FCγR) and complement receptor 3 (CR3)-mediated signaling, and potentially of other signaling pathways [106, 114, 121, 134–138].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [106]
Cites
Clustal W and Clustal X version 2.0
Larkin, M., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A., López, R., et al. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm404 · Cited by 28,221 · see citing works
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works
The phosphatidylinositol 3-Kinase–AKT pathway in human cancer
Vivanco, I., & Sawyers, C. L. (2002) · Nature reviews. Cancer · doi:10.1038/nrc839 · Cited by 6,041 · see citing works
Culture Medium for Enterobacteria
Neidhardt, F. C., Bloch, P. L., & Smith, D. F. (1974) · Journal of Bacteriology · doi:10.1128/jb.119.3.736-747.1974 · Cited by 2,977 · see citing works
Fcγ receptors as regulators of immune responses
Nimmerjahn, F., & Ravetch, J. V. (2008) · Nature Reviews Immunology · doi:10.1038/nri2206 · Cited by 2,947 · see citing works
Mechanisms of phagocytosis in macrophages
Aderem, A., & Underhill, D. M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.593 · Cited by 2,854 · see citing works
1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D. S., Bigam, C. G., Yao, J. S., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211777 · Cited by 2,361 · see citing works
Kay, L., Keifer, P. A., & Saarinen, T. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00052a088 · Cited by 2,268 · see citing works
Protein NMR Spectroscopy: Principles and Practice
Cavanagh, J. (1995) · Cited by 1,642 · see citing works
Grzesiek, S., & Bax, A. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00042a003 · Cited by 1,030 · see citing works
Protein NMR Spectroscopy. Principles and Practice
Kalbitzer, H. R. (1997) · Zeitschrift für Physikalische Chemie · doi:10.1524/zpch.1997.202.part_1_2.297 · Cited by 974 · see citing works
Araki, N., Johnson, M. T., & Swanson, J. A. (1996) · The Journal of cell biology · doi:10.1083/jcb.135.5.1249 · Cited by 949 · see citing works
Ikura, M., Kay, L. E., & Bax, A. (1990) · Biochemistry · doi:10.1021/bi00471a022 · Cited by 925 · see citing works
Wittekind, M. G., & Mueller, L. J. (1993) · Journal of Magnetic Resonance Series B · doi:10.1006/jmrb.1993.1033 · Cited by 871 · see citing works
A method for efficient isotopic labeling of recombinant proteins
Marley, J., Lu, M., & Bracken, C. (2001) · Journal of Biomolecular NMR · doi:10.1023/a:1011254402785 · Cited by 774 · see citing works
Marsh, J. A., Singh, V. K., Jia, Z., & Forman-Kay, J. D. (2006) · Protein Science · doi:10.1110/ps.062465306 · Cited by 730 · see citing works
Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis
Botelho, R. J., Teruel, M., Dierckman, R., Anderson, R., Wells, A., York, J. D., Meyer, T., & Grinstein, S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.7.1353 · Cited by 539 · cited 1× · see citing works
“C) SSP scores determined from (13)C and (13)C chemical shifts experimentally identify the helical ( 1) and strand ( 1) regions in the PH-R domain (39).”
MethodVieira, O. V., Botelho, R. J., Rameh, L. E., Brachmann, S. M., Matsuo, T., Davidson, H. W., Schreiber, A. D., Backer, J., Cantley, L. C., & Grinstein, S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200107069 · Cited by 530 · see citing works
DOWLER, S., Currie, R. A., CAMPBELL, D. G., Deák, M., Kular, G. S., Downes, C. P., & Alessi, D. R. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510019 · Cited by 516 · see citing works
Deletion of SHIP or SHP-1 Reveals Two Distinct Pathways for Inhibitory Signaling
Ono, M., Okada, H., Bolland, S. M., Yanagi, S., Kurosaki, T., & Ravetch, J. V. (1997) · Cell · doi:10.1016/s0092-8674(00)80337-2 · Cited by 488 · see citing works
p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity.
Lioubin, M. N., Algate, P. A., Tsai, S., Carlberg, K., Aebersold, A., & Rohrschneider, L. R. (1996) · Genes & Development · doi:10.1101/gad.10.9.1084 · Cited by 418 · see citing works
DOWLER, S., Currie, R. A., CAMPBELL, D. G., Maria, D. E. A. K., Kular, G. S., DOWNES, C. P., & Alessi, D. R. (2000) · Biochemical Journal · doi:10.1042/bj3510019 · Cited by 412 · see citing works
A requirement for phosphatidylinositol 3-kinase in pseudopod extension
Cox, D., Tseng, C.-C., Bjekic, G., & Greenberg, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1240 · Cited by 410 · see citing works
Cdc42, Rac1, and Rac2 Display Distinct Patterns of Activation during Phagocytosis
Hoppe, A. D., & Swanson, J. A. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-11-0847 · Cited by 365 · see citing works
DIVERGENT ROLES FOR F c RECEPTORS AND COMPLEMENT IN VIVO
Ravetch, J. V., & Clynes, R. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.421 · Cited by 360 · see citing works
The coordination of signaling during Fc receptor-mediated phagocytosis
Swanson, J. A., & Hoppe, A. D. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0804439 · Cited by 326 · see citing works
Pleckstrin homology (PH) domains and phosphoinositides
Lemmon, M. A. (2007) · Biochemical Society Symposium · doi:10.1042/bss0740081 · Cited by 298 · see citing works
Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1
Nishio, M., Watanabe, K., Sasaki, J., Taya, C., Takasuga, S., Iizuka, R., Balla, T., Yamazaki, M., Watanabe, H., Itoh, R., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1515 · Cited by 288 · see citing works
Marshall, J. G., Booth, J. W., Stambolic, V., Mak, T. W., Balla, T., Schreiber, A. D., Meyer, T., & Grinstein, S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.7.1369 · Cited by 281 · see citing works
Takeshita, S., Namba, N., Zhao, J. J., Jiang, Y., Genant, H. K., Silva, M. J., Brodt, M. D., Helgason, C. D., Kalesnikoff, J., Rauh, M. J., et al. (2002) · Nature Medicine · doi:10.1038/nm752 · Cited by 250 · see citing works
Pleckstrin homology domains: not just for phosphoinositides
Lemmon, M. A. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320707 · Cited by 229 · see citing works
Kiener, P. A., Rankin, B. M., Burkhardt, A. L., Schieven, G. L., Gilliland, L. K., Rowley, R. B., Bolen, J. B., & Ledbetter, J. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80545-6 · Cited by 196 · see citing works
Phagocytosis: measurement by flow cytometry
Lehmann, A. K., Sørnes, S., & Halstensen, A. I. (2000) · Journal of Immunological Methods · doi:10.1016/s0022-1759(00)00237-4 · Cited by 193 · see citing works
Ong, C. J., Ming‐Lum, A., Nodwell, M., Ghanipour, A., Yang, L., Williams, D. E., Kim, J., Demirjian, L., Qasimi, P., Rüschmann, J., et al. (2007) · Blood · doi:10.1182/blood-2007-03-079699 · Cited by 161 · see citing works
Self-citationYamazaki, T., Lee, W., Revington, M., Mattiello, D. L., Dahlquist, F. W., Arrowsmith, C. H., & Kay, L. E. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00093a069 · Cited by 159 · see citing works
Cox, D., Dale, B. M., Kashiwada, M., Helgason, C. D., & Greenberg, S. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.1.61 · Cited by 158 · see citing works
Brooks, R., Fuhler, G. M., Iyer, S., Smith, M. J., Park, M.-Y., Paraiso, K. H. T., Engelman, R. W., & Kerr, W. G. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902844 · Cited by 140 · see citing works
HIV-1 Tat Is a Natively Unfolded Protein
Shojania, S., & O’Neil, J. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510748200 · Cited by 132 · see citing works
Self-citationIn vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis
Dormann, D., Weijer, G., DOWLER, S., & Weijer, C. J. (2004) · Journal of Cell Science · doi:10.1242/jcs.01579 · Cited by 131 · see citing works
Inhibitor and activator: dual functions for SHIP in immunity and cancer
Kerr, W. G. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05869.x · Cited by 111 · see citing works
Coordination of Fc receptor signaling regulates cellular commitment to phagocytosis
Zhang, Y., Hoppe, A. D., & Swanson, J. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008248107 · Cited by 106 · see citing works
Sly, L. M., Rauh, M. J., Kalesnikoff, J., Büchse, T., & Krystal, G. (2003) · Experimental Hematology · doi:10.1016/j.exphem.2003.09.011 · Cited by 105 · see citing works
Huang, Z.-Y., Hunter, S., Kim, M.-K., Indik, Z. K., & Schreiber, A. D. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0902454 · Cited by 105 · see citing works
Membrane Targeting by Pleckstrin Homology Domains
Cozier, G. E., Carlton, J. G., Bouyoucef, D., & Cullen, P. (2004) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-18805-3_3 · Cited by 91 · see citing works
Receptor mobility, the cytoskeleton, and particle binding during phagocytosis
Jaumouillé, V., & Grinstein, S. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.10.006 · Cited by 84 · see citing works
Differential Association of Phosphatidylinositol 3-Kinase, SHIP-1, and PTEN with Forming Phagosomes
Kamen, L. A., Levinsohn, J. L., & Swanson, J. A. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0061 · Cited by 79 · see citing works
Dewitt, S., Tian, W., & Hallett, M. B. (2006) · Journal of Cell Science · doi:10.1242/jcs.02756 · Cited by 76 · see citing works
SHIP deficiency causes Crohn's disease-like ileitis
Kerr, W. G., Park, M.-Y., Maubert, M., & Engelman, R. W. (2010) · Gut · doi:10.1136/gut.2009.202283 · Cited by 74 · see citing works
SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation
Damen, J. E., Ware, M. D., Kalesnikoff, J., Hughes, M. R., & Krystal, G. (2001) · Blood · doi:10.1182/blood.v97.5.1343 · Cited by 71 · see citing works
Regulation of the immune response by SHIP
March, M., & Ravichandran, K. S. (2002) · Seminars in Immunology · doi:10.1006/smim.2001.0340 · Cited by 66 · see citing works
Keightley, D. D., & Cressie, N. (1980) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(80)90092-8 · Cited by 64 · see citing works
Aman, M. J., Walk, S. F., March, M., Su, H.-P., Carver, D. J., & Ravichandran, K. S. (2000) · Molecular and Cellular Biology · doi:10.1128/.20.10.3576-3589.2000 · Cited by 61 · see citing works
Gupta, N., Scharenberg, A. M., Fruman, D. A., Cantley, L. C., Kinet, J.-P., & Long, E. O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.11.7489 · Cited by 60 · see citing works
Ganesan, L. P., Fang, H., Marsh, C. B., & Tridandapani, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305078200 · Cited by 57 · see citing works
SHIP-Deficient Mice Develop Spontaneous Intestinal Inflammation and Arginase-Dependent Fibrosis
McLarren, K. W., Cole, A. E., Weisser, S. B., Voglmaier, N., Conlin, V. S., Jacobson, K., Popescu, O., Boucher, J., & Sly, L. M. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.03.018 · Cited by 54 · see citing works
Ai, J., Maturu, A., Johnson, W., Wang, Y., Marsh, C. B., & Tridandapani, S. (2005) · Blood · doi:10.1182/blood-2005-05-1841 · Cited by 50 · see citing works
Blasi, E., Radzioch, D., Merletti, L., & Varesio, L. (1989) · PubMed · Cited by 48 · see citing works
Evidence That the Lipid Phosphatase SHIP-1 Regulates T Lymphocyte Morphology and Motility
Harris, S. J., Parry, R. V., Foster, J. G., Blunt, M. D., Wang, A., Marelli‐Berg, F. M., Westwick, J. K., & Ward, S. G. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002350 · Cited by 34 · see citing works
Activation of SHIP via a small molecule agonist kills multiple myeloma cells
Kennah, M., Yau, T. Y., Nodwell, M., Krystal, G., Andersen, R. J., Ong, C. J., & Mui, A. (2009) · Experimental Hematology · doi:10.1016/j.exphem.2009.08.001 · Cited by 32 · see citing works
Self-citationEdlich, C., Stier, G., Simon, B., Sattler, M., & Muhle‐Goll, C. (2005) · Structure · doi:10.1016/j.str.2004.11.012 · Cited by 29 · see citing works
Yogo, K., Mizutamari, M., Mishima, K., Takenouchi, H., Ishida‐Kitagawa, N., Sasaki, T., & Takeya, T. (2006) · Endocrinology · doi:10.1210/en.2005-1309 · Cited by 27 · see citing works
Wada, T., Sasaoka, T., Ishiki, M., Hori, H., Haruta, T., Ishihara, H., & Kobayashi, M. (1999) · Endocrinology · doi:10.1210/endo.140.10.7028 · Cited by 22 · see citing works
Wientjes, F. B., & Segal, A. W. (2003) · Current Opinion in Hematology · doi:10.1097/00062752-200301000-00002 · Cited by 20 · see citing works
MacDonald, S. M., & Vonakis, B. M. (2002) · Molecular Immunology · doi:10.1016/s0161-5890(02)00082-2 · Cited by 17 · see citing works
LyGDI, a Novel SHIP-Interacting Protein, Is a Negative Regulator of FcγR-Mediated Phagocytosis
Mehta, P., Wavreille, A., Justiniano, S. E., Marsh, R. L., Yu, J., Burry, R. W., Jarjoura, D. G., Eubank, T. D., Caligiuri, M. A., Butchar, J. P., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021175 · Cited by 13 · see citing works
Flagged first, then by citations
1 of the 66 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Of ITIM s, ITAM s, and ITAM is: revisiting immunoglobulin Fc receptor signaling
Getahun, A., & Cambier, J. C. (2015) · Immunological Reviews · doi:10.1111/imr.12336 · Cited by 163 · see citing works
Foster, J. G., Blunt, M. D., Carter, E. P., & Ward, S. G. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.004051 · Cited by 121 · see citing works
Pauls, S. D., & Marshall, A. J. (2017) · European Journal of Immunology · doi:10.1002/eji.201646795 · Cited by 118 · see citing works
Terzioglu, G., & Young-Pearse, T. L. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00674-9 · Cited by 95 · see citing works
Activation/Inhibition of mast cells by supra-optimal antigen concentrations
Huber, M. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-7 · Cited by 54 · see citing works
Role of SHIP1 in cancer and mucosal inflammation
Fernandes, S. R. M., Iyer, S., & Kerr, W. G. (2013) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12038 · Cited by 41 · see citing works
Chamberlain, T. C., Cheung, S. T., Yoon, J. S. J., Ming-Lum, A., Gardill, B. R., Shakibakho, S., Dzananovic, E., Ban, F., Samiea, A., Jawanda, K., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101433 · Cited by 32 · see citing works
Self-citationRole of inositol phospholipid signaling in natural killer cell biology
Gumbleton, M., & Kerr, W. G. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00047 · Cited by 31 · see citing works
Role of inhibitory signaling in peripheral B cell tolerance*
Getahun, A. (2022) · Immunological Reviews · doi:10.1111/imr.13070 · Cited by 29 · see citing works
SHIP2 signalling at the plasma membrane, in the nucleus and at focal contacts
Edimo, W. E., Vanderwinden, J., & Erneux, C. (2012) · Advances in Biological Regulation · doi:10.1016/j.jbior.2012.09.003 · Cited by 29 · see citing works
PtdIns(3,4)P2, Lamellipodin, and VASP coordinate actin dynamics during phagocytosis in macrophages
Montaño-Rendón, F., Walpole, G. F. W., Krause, M., Hammond, G. R. V., Grinstein, S., & Fairn, G. D. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202207042 · Cited by 23 · see citing works
Waddell, G. L., Drew, E. E., Rupp, H. P., & Hansen, S. D. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105022 · Cited by 19 · see citing works
Blunt, M. D., & Ward, S. G. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00226 · Cited by 19 · see citing works
SHIP negatively regulates type II immune responses in mast cells and macrophages
Dobranowski, P., & Sly, L. M. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mir0817-340r · Cited by 19 · see citing works
INPP5D/SHIP1: Expression, Regulation and Roles in Alzheimer’s Disease Pathophysiology
Olufunmilayo, E. O., & Holsinger, R. M. D. (2023) · Genes · doi:10.3390/genes14101845 · Cited by 19 · see citing works
A new layer of phosphoinositide‐mediated allosteric regulation uncovered for SHIP2
Coq, J. L., Navajas, P. L., Martín, B. R., Alfonso, C., & Lietha, D. (2021) · The FASEB Journal · doi:10.1096/fj.202100561r · Cited by 17 · see citing works
Pauls, S. D., Ray, A., Hou, S., Vaughan, A. T., Cragg, M. S., & Marshall, A. J. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1600105 · Cited by 16 · see citing works
Huber, M., & Gibbs, B. F. (2014) · Molecular Immunology · doi:10.1016/j.molimm.2014.02.017 · Cited by 13 · see citing works
Müller, S., Nelson, N., & Jücker, M. (2025) · Biomolecules · doi:10.3390/biom15010105 · Cited by 9 · see citing works
Expression, purification and characterization of the RhoA-binding domain of human SHIP2 in E.coli
Zhou, H., Yue, X., Wang, Z., Li, S., Zhu, J., Yang, Y., & Liu, M. (2021) · Protein Expression and Purification · doi:10.1016/j.pep.2021.105821 · Cited by 9 · see citing works
The Inositol-5-Phosphatase SHIP1: Expression, Regulation and Role in Acute Lymphoblastic Leukemia
Ehm, P. A. H., & Jücker, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146935 · Cited by 5 · see citing works
Rasmussen, P., Spillner, E., & Hoffmann, H. J. (2019) · Immunology Letters · doi:10.1016/j.imlet.2019.04.003 · Cited by 5 · see citing works
INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia
Terzioglu, G., Karp, E. S., Heuer, S. E., Chadarevian, J. P., Ahsan, F. M., Haage, V. C., Davtyan, H., Fogo, G. M., Curle, A. J., Ashour, N., et al. (2025) · doi:10.1101/2025.10.27.684632 · Cited by 3 · see citing works
Wang, Z., Shan, Y., Wang, R., Zhou, H., Hu, R., Li, Y., Zhu, J., Yang, Y., & Liu, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911299 · Cited by 3 · see citing works
Coq, J. L., Gallego, L. H., & Lietha, D. (2016) · The Protein Journal · doi:10.1007/s10930-016-9665-y · Cited by 3 · see citing works
Regulation of FcεRI Signaling by Lipid Phosphatases
Kuhny, M., Zorn, C. N., & Huber, M. (2014) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-07911-0_6 · Cited by 3 · see citing works
Panah, A. K., & Jaumouillé, V. (2025) · Elsevier eBooks · doi:10.1016/b978-0-12-824465-4.00199-x · Cited by 1 · see citing works
A new paradigm in phosphoinositide signaling? (Comment on DOI 10.1002/bies.201100195)
So, E., & Mui, A. (2012) · BioEssays · doi:10.1002/bies.201200091 · Cited by 1 · see citing works
Self-citationIdentification of SHIP-1 and SHIP-2 homologs in channel catfish, Ictalurus punctatus
Taylor, E. B., Nayak, D. K., Quiniou, S. M. A., Bengtén, E., & Wilson, M. (2015) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2015.02.015 · Cited by 1 · see citing works
Wang, T. (2016) · cIRcle (University of British Columbia) · doi:10.14288/1.0223580
Defining microglial phenotypic diversity and the impact of ageing
Grabert, K. (2015) · ERA
Mechanisms controlling membrane recruitment and activation of autoinhibited SHIP1Preprint
Waddell, G. L., Drew, E. E., Rupp, H. P., & Hansen, S. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.30.538895
Structural insights into SHIP2 reveal its membrane regulatory mechanisms
Gupta, J., Coq, J. L., Lietha, D., & Izard, T. (2026) · Protein Science · doi:10.1002/pro.70479
Functional role of the second messengers PtdIns(3,4,5)P 3 and PtdIns(3,4)P 2 in carcinogenesis
Nelson, N., & Jücker, M. (2026) · Biological Chemistry · doi:10.1515/hsz-2026-0181
- Authors
- Ming‐Lum, A., Shojania, S., So, E., McCarrell, E., Shaw, E., Vu, D., Wang, I., McIntosh, L. P., & Mui, A. L. ‐.
- Affiliations
- University of British Columbia (CA)
- Corresponding author
- Mui, Alice L.‐F.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2012-05-31
- Volume
- 26
- Issue
- 8
- Pages
- 3163-3177
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2096968286
- Cited by
- 34
- References
- 66
- Citations by year
- 2026: 2 · 2025: 4 · 2023: 4 · 2022: 3 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 3 · 2014: 2 · 2013: 3 · 2012: 4
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research
- Canada Foundation for Innovation
- British Columbia Knowledge Development Fund
- Michael Smith Foundation for Health Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- SHIP1, membrane localization, phosphatidylinositol 3,4,5-trisphosphate, Fc gamma receptor, phagocytosis, macrophages, inflammation reduction, phosphatidylinositol 3-kinase
- MeSH terms
- Inositol Polyphosphate 5-Phosphatases, Allosteric Regulation, Amino Acid Sequence, Phagocytosis, Phosphoric Monoester Hydrolases, Protein Structure, Tertiary, Receptors, IgG, Phosphatidylinositol Phosphates, Nuclear Magnetic Resonance, Biomolecular
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
