Biopolym. Cell. 2015; 31(5):395-401.
Короткі повідомлення
Нові партнери скафолдного білка TKS4
1Кропивко С. В.
  1. Інститут молекулярної біології і генетики НАН України
    Вул. Академіка Заболотного, 150, Київ, Україна, 03680

Abstract

Скафолд TKS4 бере участь у формуванні інвадоподій, продукції активних форм кисню (ROS) в ракових клітинах та інших клітинних процесах. Мета. Ідентифікувати нових партнерів TKS4, задіяних в перебудовах актинового цитоскелету та ендо-/екзоцитозі. Методи. In vitro GST pull-down assay. Результати. Показано, що SH3 домени TKS4 взаємодіють з білками-реорганізаторами актинового цитоскелету N-WASP та CR16, а також з DNM2, SYNJ1 та OPHN1, які задіяні в ендо-/екзоцитозі. Проте взаємодії WIP, WIRE, SHIP2, RhoU, RhoV та NUMB, з SH3 доменами TKS4 не знайдено. Висновки. SH3 домени TKS4 взаємодіють з білками N-WASP, DNM2, SYNJ1, OPHN1 та слабко з CR16 in vitro.
Keywords: TKS4, адаптерні/скафолдні білки, актиновий цитоскелет, ендо-/екзоцитоз

References

[1] Pawson T. Dynamic control of signaling by modular adaptor proteins. Curr Opin Cell Biol. 2007;19(2):112-6.
[2] Reebye V, Frilling A, Hajitou A, Nicholls JP, Habib NA, Mintz PJ. A perspective on non-catalytic Src homology (SH) adaptor signalling proteins. Cell Signal. 2012;24(2):388-92.
[3] Balla T. Inositol-lipid binding motifs: signal integrators through protein-lipid and protein-protein interactions. J Cell Sci. 2005;118(Pt 10):2093-104.
[4] Buschman MD, Bromann PA, Cejudo-Martin P, Wen F, Pass I, Courtneidge SA. The novel adaptor protein Tks4 (SH3PXD2B) is required for functional podosome formation. Mol Biol Cell. 2009;20(5):1302-11.
[5] Lányi Á, Baráth M, Péterfi Z, Bogel G, Orient A, Simon T, Petrovszki E, Kis-Tóth K, Sirokmány G, Rajnavölgyi É, Terhorst C, Buday L, Geiszt M. The homolog of the five SH3-domain protein (HOFI/SH3PXD2B) regulates lamellipodia formation and cell spreading. PLoS One. 2011;6(8):e23653.
[6] Gianni D, Diaz B, Taulet N, Fowler B, Courtneidge SA, Bokoch GM. Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity. Sci Signal. 2009;2(88):ra54.
[7] Gianni D, Taulet N, DerMardirossian C, Bokoch GM. c-Src-mediated phosphorylation of NoxA1 and Tks4 induces the reactive oxygen species (ROS)-dependent formation of functional invadopodia in human colon cancer cells. Mol Biol Cell. 2010;21(23):4287-98.
[8] Hishida T, Eguchi T, Osada S, Nishizuka M, Imagawa M. A novel gene, fad49, plays a crucial role in the immediate early stage of adipocyte differentiation via involvement in mitotic clonal expansion. FEBS J. 2008;275(22):5576-88.
[9] Bendon CL, Fenwick AL, Hurst JA, Nürnberg G, Nürnberg P, Wall SA, Wilkie AO, Johnson D. Frank-ter Haar syndrome associated with sagittal craniosynostosis and raised intracranial pressure. BMC Med Genet. 2012;13:104.
[10] Wilson GR, Sunley J, Smith KR, Pope K, Bromhead CJ, Fitzpatrick E, Di Rocco M, van Steensel M, Coman DJ, Leventer RJ, Delatycki MB, Amor DJ, Bahlo M, Lockhart PJ. Mutations in SH3PXD2B cause Borrone dermato-cardio-skeletal syndrome. Eur J Hum Genet. 2014;22(6):741–7.
[11] Mao M, Solivan-Timpe F, Roos BR, Mullins RF, Oetting TA, Kwon YH, Brzeskiewicz PM, Stone EM, Alward WL, Anderson MG, Fingert JH. Localization of SH3PXD2B in human eyes and detection of rare variants in patients with anterior segment diseases and glaucoma. Mol Vis. 2012;18:705-13.
[12] Mao M, Thedens DR, Chang B, Harris BS, Zheng QY, Johnson KR, Donahue LR, Anderson MG. The podosomal-adaptor protein SH3PXD2B is essential for normal postnatal development. Mamm Genome. 2009;20(8):462-75.
[13] Havrylov S, Rzhepetskyy Y, Malinowska A, Drobot L, Redowicz MJ. Proteins recruited by SH3 domains of Ruk/CIN85 adaptor identified by LC-MS/MS. Proteome Sci. 2009;7:21.
[14] Bisson N, James DA, Ivosev G, Tate SA, Bonner R, Taylor L, Pawson T. Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor. Nat Biotechnol. 2011;29(7):653-8.
[15] Murphy DA, Courtneidge SA. The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function. Nat Rev Mol Cell Biol. 2011;12(7):413-26.
[16] Kropyvko S, Gerasymchuk D, Skrypkina I, Dergai M, Dergai O, Nikolaienko O, Rynditch A, Tsyba L. Structural diversity and differential expression of novel human intersectin 1 isoforms. Mol Biol Rep. 2010;37(6):2789–96.
[17] Tsyba L, Gryaznova T, Dergai O, Dergai M, Skrypkina I, Kropyvko S, Boldyryev O, Nikolaienko O, Novokhatska O, Rynditch A. Alternative splicing affecting the SH3A domain controls the binding properties of intersectin 1 in neurons. Biochem Biophys Res Commun. 2008;372(4):929-34.
[18] 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;27(7):1499-508.
[19] Gubar OS, Houy S, Billuart P, Kropyvko SV, Tsyba LO, Gasman S, Rynditch AV. GTPase-activating protein oligophrenin 1 is a new partner of multifunctional adapter protein intersectin 1. Biopolym Cell. 2012;28(5):357–362.
[20] Colaluca IN, Tosoni D, Nuciforo P, Senic-Matuglia F, Galimberti V, Viale G, Pece S, Di Fiore PP. NUMB controls p53 tumour suppressor activity. Nature. 2008;451(7174):76–80.
[21] Dyson JM, O'Malley CJ, Becanovic J, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA. The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol. 2001;155(6):1065–79.
[22] Saras J, Wollberg P, Aspenström P. Wrch1 is a GTPase-deficient Cdc42-like protein with unusual binding characteristics and cellular effects. Exp Cell Res. 2004;299(2):356-69.
[23] Aspenström P, Ruusala A, Pacholsky D. Taking Rho GTPases to the next level: the cellular functions of atypical Rho GTPases. Exp Cell Res. 2007;313(17):3673-9.
[24] González-Jamett AM, Momboisse F, Guerra MJ, Ory S, Báez-Matus X, Barraza N, Calco V, Houy S, Couve E, Neely A, Martínez AD, Gasman S, Cárdenas AM. Dynamin-2 regulates fusion pore expansion and quantal release through a mechanism that involves actin dynamics in neuroendocrine chromaffin cells. PLoS One. 2013;8(8):e70638.
[25] Xie J, Vandenbroere I, Pirson I. SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF. FEBS Lett. 2008;582(20):3011-7.
[26] Aspenström P. The verprolin family of proteins: regulators of cell morphogenesis and endocytosis. FEBS Lett. 2005;579(24):5253-9.
[27] Nakano-Kobayashi A, Kasri NN, Newey SE, Van Aelst L. The Rho-linked mental retardation protein OPHN1 controls synaptic vesicle endocytosis via endophilin A1. Curr Biol. 2009;19(13):1133-9.
[28] McMahon HT, Boucrot E. Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat Rev Mol Cell Biol. 2011;12(8):517-33.
[29] Faure S, Fort P. Atypical RhoV and RhoU GTPases control development of the neural crest. Small GTPases. 2011;2(6):310-313.
[30] Drouet V, Lesage S. Synaptojanin 1 mutation in Parkinson's disease brings further insight into the neuropathological mechanisms. Biomed Res Int. 2014;2014:289728.