The interaction of verprolin WIRE with the adapter proteins family intersectin

  • S. V. Kropyvko Institute of Molecular Biology and Genetics of Natl. Acad. Sci. of Ukraine, Ukraine, 03143, Kyiv, Akad. Zabolotnogo str., 150
  • A. V. Rynditch Institute of Molecular Biology and Genetics of Natl. Acad. Sci. of Ukraine, Ukraine, 03143, Kyiv, Akad. Zabolotnogo str., 150

Abstract

Aim. WIRE is a scafold protein that regulates actin cytoskeleton rearrangements and the formation of actin enriched membrane processes responsible for invasion and migration. ITSN1 and ITSN2 are representatives of the family of intersectins who participate in the reorganization of the actin cytoskeleton, as well as in other processes, such as endo/enzocytosis, cellular signal transduction, etc. As these proteins participate in the same processes, we checked their interaction with each other. Methods. Protein-protein interactions were identified using the GST pull-down method. Results. We showed that the SH3 domains of ITSN1 and ITSN2 interact with WIRE, and found that while WIRE is in a complex with endogenous actin. Conclusions. ITSN1 and ITSN2 interact with WIRE, which is located in a complex with endogenous actin.
Keywords: WIRE, ITSN1 and ITSN2, actin.

References

Aspenström P. The WASP-binding protein WIRE has a role in the regulation of the actin filament system downstream of the platelet-derived growth factor. Exp. Cell Res. 2002. Vol. 279(1). P. 21–33. doi: 10.1006/excr.2002.5576

Aspenstrom P. The mammalian verprolin homologue WIRE participates in receptor-mediated endocytosis and regulation of the actin filament system by distinct mechanisms. Exp. Cell Res. 2004. Vol. 298(2). P. 485–498. doi: 10.1016/j.yexcr.2004.04.050

Dominguez R., Holmes K.C. Actin structure and function. Annu. Rev. Biophys. 2011. Vol. 40. P. 169–186. doi: 10.1146/annurev-biophys-042910-155359

García E., Ragazzini C., Yu X., Cuesta-García E., Bernardino de la Serna J., Zech T., Sarrió D., Machesky L.M., Antón I.M. WIP and WICH/WIRE co-ordinately control invadopodium formation and maturation in human breast cancer cell invasion. Sci. Rep. 2016. Vol. 6. P. 23590. doi: 10.1038/srep23590

Gryaznova T., Kropyvko S., Burdyniuk M., Gubar O., Kryklyva V., Tsyba L., Rynditch A. Intersectin adaptor proteins are associated with actin-regulating protein WIP in invadopodia. Cell Signal. 2015. Vol. 27(7). P. 1499-1508. doi: 10.1016/j.cellsig.2015.03.006

Ho H.H., Rohatgi R., Ma L., Kirschner M.W. CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family. Proc. Natl. Acad. Sci. U S A. 2001. Vol. 98(20). P. 11306–11311. doi: 10.1073/pnas.211420498

Hussain N.K., Jenna S., Glogauer M., Quinn C.C., Wasiak S., Guipponi M., Antonarakis S.E., Kay B.K., Stossel T.P., Lamarche-Vane N., McPherson P.S. Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP. Nat. Cell. Biol. 2001. Vol. 3(10). P. 927–932. doi: 10.1038/ncb1001-927

Jenna S., Hussain N.K., Danek E.I., Triki I., Wasiak S., McPherson P.S., Lamarche-Vane N. The activity of the GTPase-activating protein CdGAP is regulated by the endocytic protein intersectin. J. Biol. Chem. 2002. Vol. 277(8). P. 6366–6373. doi: 10.1074/jbc.M105516200

Kato M., Miki H., Kurita S., Endo T., Nakagawa H., Miyamoto S., Takenawa T. WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation. Biochem. Biophys. Res. Commun. 2002. Vol. 291(1). P. 41–47. doi: 10.1006/bbrc.2002.6406

Kato M., Takenawa T. WICH, a member of WASP-interacting protein family, cross-links actin filaments. Biochem. Biophys. Res. Commun. 2005. Vol. 328(4). P. 1058–1066. doi: 10.1016/j.bbrc.2005.01.058

Klein I.K., Predescu D.N., Sharma T., Knezevic I., Malik A.B., Predescu S. Intersectin-2L regulates caveola endocytosis secondary to Cdc42-mediated actin polymerization. J. Biol. Chem. 2009. Vol. 284(38). P. 25953–25961.

Kropyvko S., Gryaznova T., Morderer D., Rynditch A. Mammalian verprolin CR16 acts as a modulator of ITSN scaffold proteins association with actin. Biochem Biophys Res Commun. 2017. Vol. 484(4). P. 813-819. doi: 10.1016/j.bbrc.2017.01.177

McGavin M.K.H., Badour K., Hardy L.A., Kubiseski T.J., Zhang J., Siminovitch K.A. The intersectin 2 adaptor links Wiskott Aldrich syndrome protein (WASp)-mediated actin polymerization to T cell antigen receptor endocytosis. J. Exp. Med. 2001. Vol. 194(12). P. 1777–1787.

Misra A., Rajmohan R., Lim R.P., Bhattacharyya S., Thanabalu T. The mammalian Verprolin, WIRE induces filopodia independent of N-WASP through IRSp53. Exp Cell Res. 2010. Vol. 316(17). P. 2810-2824. doi: 10.1016/j.yexcr.2010.07.015

Novokhatska O., Dergai M., Tsyba L., Skrypkina I., Filonenko V., Moreau J., Rynditch A. Adaptor proteins intersectin 1 and 2 bind similar proline-rich ligands but are differentially recognized by SH2 domain-containing proteins. PLoS One. 2013. Vol. 8(7). P. e70546. doi: 10.1371/journal.pone.0070546

O'Bryan J.P. Intersecting pathways in cell biology. Sci. Signal. 2010. Vol. 3(152). P. re10. doi: 10.1126/scisignal.3152re10.

Pucharcos C., Casas C., Nadal M., Estivill X., de la Luna S. The human intersectin genes and their spliced variants are differentially expressed. Biochim. Biophys. Acta. 2001. Vol. 1521. P. 1–11. doi: 10.1016/S0167-4781(01)00276-7

Rossman K.L., Der C.J., Sondek J. GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat. Rev. Mol. Cell Biol. 2005. Vol. 6(2). P. 167–180. doi: 10.1038/nrm1587

Sasahara Y., Rachid R., Byrne M.J., de la Fuente M.A., Abraham R.T., Ramesh N., Geha R.S. Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation. Mol. Cell. 2002. Vol. 10(6). P. 1269–1281. doi: 10.1016/S1097-2765(02)00728-1

Sengar A.S., Wang W., Bishay J., Cohen S., Egan S.E. The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15. EMBO J. 1999. Vol. 18(5). P. 1159–1171. doi: 10.1093/emboj/18.5.1159

Tsyba L., Nikolaienko O., Dergai O., Dergai M., Novokhatska O., Skrypkina I., Rynditch A. Intersectin multidomain adaptor proteins: regulation of functional diversity. Gene. 2011. Vol. 473(2). P. 67–75. doi: 10.1016/j.gene.2010.11.016

Weiler M.C., Smith J.L., Masters J.N. CR16, a novel proline-rich protein expressed in rat brain neurons, binds to SH3 domains and is a MAP kinase substrate. J. Mol. Neurosci. Fall. 1996. Vol. 7(3). P. 203–215

Wong K.A., Wilson J., Russo A., Wang L., Okur M.N., Wang X., Martin N.P., Scappini E., Carnegie G.K., O'Bryan J.P. Intersectin (ITSN) family of scaffolds function as molecular hubs in protein interaction networks. PLoS ONE. 2012. Vol. 7(4). P. e36023. doi: 10.1371/journal.pone.0036023

Yamaguchi H., Lorenz M., Kempiak S., Sarmiento C., Coniglio S., Symons M., Segall J., Eddy R., Miki H., Takenawa T., Condeelis J. Molecular mechanisms of invadopodium formation: the role of the N-WASP-Arp2/3 complex pathway and cofilin. J. Cell Biol. 2005. Vol. 168(3). P. 441–452. doi: 10.1083/jcb.200407076