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The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin.
J Cell Biol. 2001 Dec 10; 155(6):1065-79.JC

Abstract

SHIP-2 is a phosphoinositidylinositol 3,4,5 trisphosphate (PtdIns[3,4,5]P3) 5-phosphatase that contains an NH2-terminal SH2 domain, a central 5-phosphatase domain, and a COOH-terminal proline-rich domain. SHIP-2 negatively regulates insulin signaling. In unstimulated cells, SHIP-2 localized in a perinuclear cytosolic distribution and at the leading edge of the cell. Endogenous and recombinant SHIP-2 localized to membrane ruffles, which were mediated by the COOH-terminal proline-rich domain. To identify proteins that bind to the SHIP-2 proline-rich domain, yeast two-hybrid screening was performed, which isolated actin-binding protein filamin C. In addition, both filamin A and B specifically interacted with SHIP-2 in this assay. SHIP-2 coimmunoprecipitated with filamin from COS-7 cells, and association between these species did not change after epidermal growth factor stimulation. SHIP-2 colocalized with filamin at Z-lines and the sarcolemma in striated muscle sections and at membrane ruffles in COS-7 cells, although the membrane ruffling response was reduced in cells overexpressing SHIP-2. SHIP-2 membrane ruffle localization was dependent on filamin binding, as SHIP-2 was expressed exclusively in the cytosol of filamin-deficient cells. Recombinant SHIP-2 regulated PtdIns(3,4,5)P3 levels and submembraneous actin at membrane ruffles after growth factor stimulation, dependent on SHIP-2 catalytic activity. Collectively these studies demonstrate that filamin-dependent SHIP-2 localization critically regulates phosphatidylinositol 3 kinase signaling to the actin cytoskeleton.

Authors+Show Affiliations

Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, 3800 Australia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11739414

Citation

Dyson, J M., et al. "The SH2-containing Inositol Polyphosphate 5-phosphatase, SHIP-2, Binds Filamin and Regulates Submembraneous Actin." The Journal of Cell Biology, vol. 155, no. 6, 2001, pp. 1065-79.
Dyson JM, O'Malley CJ, Becanovic J, et al. The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol. 2001;155(6):1065-79.
Dyson, J. M., O'Malley, C. J., Becanovic, J., Munday, A. D., Berndt, M. C., Coghill, I. D., Nandurkar, H. H., Ooms, L. M., & Mitchell, C. A. (2001). The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. The Journal of Cell Biology, 155(6), 1065-79.
Dyson JM, et al. The SH2-containing Inositol Polyphosphate 5-phosphatase, SHIP-2, Binds Filamin and Regulates Submembraneous Actin. J Cell Biol. 2001 Dec 10;155(6):1065-79. PubMed PMID: 11739414.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. AU - Dyson,J M, AU - O'Malley,C J, AU - Becanovic,J, AU - Munday,A D, AU - Berndt,M C, AU - Coghill,I D, AU - Nandurkar,H H, AU - Ooms,L M, AU - Mitchell,C A, Y1 - 2001/12/10/ PY - 2001/12/12/pubmed PY - 2002/1/16/medline PY - 2001/12/12/entrez SP - 1065 EP - 79 JF - The Journal of cell biology JO - J Cell Biol VL - 155 IS - 6 N2 - SHIP-2 is a phosphoinositidylinositol 3,4,5 trisphosphate (PtdIns[3,4,5]P3) 5-phosphatase that contains an NH2-terminal SH2 domain, a central 5-phosphatase domain, and a COOH-terminal proline-rich domain. SHIP-2 negatively regulates insulin signaling. In unstimulated cells, SHIP-2 localized in a perinuclear cytosolic distribution and at the leading edge of the cell. Endogenous and recombinant SHIP-2 localized to membrane ruffles, which were mediated by the COOH-terminal proline-rich domain. To identify proteins that bind to the SHIP-2 proline-rich domain, yeast two-hybrid screening was performed, which isolated actin-binding protein filamin C. In addition, both filamin A and B specifically interacted with SHIP-2 in this assay. SHIP-2 coimmunoprecipitated with filamin from COS-7 cells, and association between these species did not change after epidermal growth factor stimulation. SHIP-2 colocalized with filamin at Z-lines and the sarcolemma in striated muscle sections and at membrane ruffles in COS-7 cells, although the membrane ruffling response was reduced in cells overexpressing SHIP-2. SHIP-2 membrane ruffle localization was dependent on filamin binding, as SHIP-2 was expressed exclusively in the cytosol of filamin-deficient cells. Recombinant SHIP-2 regulated PtdIns(3,4,5)P3 levels and submembraneous actin at membrane ruffles after growth factor stimulation, dependent on SHIP-2 catalytic activity. Collectively these studies demonstrate that filamin-dependent SHIP-2 localization critically regulates phosphatidylinositol 3 kinase signaling to the actin cytoskeleton. SN - 0021-9525 UR - https://www.unboundmedicine.com/medline/citation/11739414/The_SH2_containing_inositol_polyphosphate_5_phosphatase_SHIP_2_binds_filamin_and_regulates_submembraneous_actin_ L2 - https://rupress.org/jcb/article-lookup/doi/10.1083/jcb.200104005 DB - PRIME DP - Unbound Medicine ER -