ORIGINAL ARTICLES
A likely role for a novel PH-domain containing protein, PEPP2, in connecting membrane and cytoskeleton
Yi Zou and Wenping Zhong
Department of Biology, School of Life Science and Technology, Jinan University, Guangzhou, China
Address correspondence to:
Yi Zou.
Department of Biology, School of Life Science and Technology, Jinan University,
Guangzhou 510632, R.P. China. E-mail: tyizou@jnu.edu.cn
ABSTRACT: PH domains (pleckstrin homology) are well known to bind membrane phosphoinositides with different specificities and direct PH domain-containing proteins to discrete subcellular apartments with assistances of alternative binding partners. PH domain-containing proteins are found to be involved in a wide range of cellular events, including signalling, cytoskeleton rearrangement and vesicular trafficking. Here we showed that a novel PH domain-containing protein, PEPP2, displayed moderate phosphoinositide binding specificity. Full length PEPP2 associated with both plasma membrane and microtubules. The membrane-associated PEPP2 nucleated at cell-cell contacts and the leading edge of migrating cells. Overexpression of PEPP2 increased membrane microviscosity, indicating a potential role of PEPP2 in regulating function of membrane and microtubules.
Key words: Microtubule; Membrane; Phosphoinositide; Microviscosity; Wortmannin
El texto del artículo fue retirado el 5 de Mayo de 2014 a solicitud del editor.
The text of this article was removed on May, 5th by request of the chief editor.
References
1. Chang JY, He RY, Lin HP, Hsu LJ, Lai FJ, Hong Q, Chen SJ, Chang NS (2010). Signaling from membrane receptors to tumor suppressor WW domain-containing oxidoreductase. Experimental Biology and Medicine 235: 796-804.
2. Dowler S, Currie RA, Campbell DG, Deak M, Kular G, Downes CP, Alessi DR (2000). Identification of pleckstrin-homologydomain-containing proteins with novel phosphoinositide-binding specificities. Biochemical Journal 351: 19-31.
3. Ghosh PK, Vasanji A, Murugesan G, Eppell SJ, Graham LM, Fox PL (2002). Membrane microviscosity regulates endothelial cell motility. Nature Cell Biology 4: 894-900.
4. Gundersen GG, Bretscher A (2003). Cell biology. Microtubule asymmetry. Science 300: 2040-2041.
5. Insall RH, Weiner OD (2001). PIP3, PIP2, and cell movement- similar messages, different meanings? Developmental Cell 1: 743-747.
6. Lemmon MA, Ferguson KM, Abrams CS (2002). Pleckstrin homology domains and the cytoskeleton. FEBS Letters 513: 71-76.
7. Mayer U, Jürgens G (2002). Microtubule cytoskeleton: a track record. Current Opinion in Plant Biology 5: 494-501.
8. Nabi IR (1999). The polarization of the motile cell. Journal of Cell Science 112: 1803-11.
9. Rodriguez OC, Schaefer AW, Mandato CA, Forscher P, Bement WM, Waterman-Storer CM (2003). Conserved microtubule-actin interactions in cell movement and morphogenesis. Nature Cell Biology 5: 599-609.
10. Russo C, Gao Y, Mancini P, Vanni C, Porotto M, Falasca M, Torrisi MR, Schroer TA (2000). Motors, clutches and brakes for membrane traffic: a commemorative review in honor of Thomas Kreis. Traffic 1: 3-10.
11. Simonsen A, Lippe R, Christoforidis S, Gaullier JM, Brech A, Callaghan J, Toh BH, Murphy C, Zerial M, Stenmark H (1998). EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 394: 494-498.
12. Tall EG, Spector I, Pentyala SN, Bitter I, Rebecchi MJ (2000). Dynamics of phosphatidylinositol 4,5-bisphosphate in actinrich structures. Current Biology 10: 743-746.
13. Tyers M, Rachubinski RA, Stewart MI, Varrichio AM, Shorr RG, Haslam RJ, Harley CB (1988). Molecular cloning and expression of the major protein kinase C substrate of platelets. Nature 333: 470-473.
14. Vereb G, Szöllosi J, Matkó J, Nagy P, Farkas T, Vigh L, Mátyus L, Waldmann TA, Damjanovich S (2003). Dynamic, yet structured: The cell membrane three decades after the Singer-Nicolson model. Proceedings of the National Academy of Sciences (USA) 100: 8053-8058.
Received: April 13, 2012.
Revised version received: August 7, 2012.
Accepted: October 10, 2012.