The involvement of Abl and PTP61F in the regulation of Abi protein localization and stability and lamella formation in Drosophila S2 cells.

作者: Chiu-Hui Huang , Tzu-Yang Lin , Rong-Long Pan , Jyh-Lyh Juang

DOI: 10.1074/JBC.M702583200

关键词:

摘要: Most aspects of cellular events are regulated by a series protein phosphorylation and dephosphorylation processes. Abi (Abl interactor protein) functions as substrate adaptor for Abl core member the WAVE complex, relaying signals from Rac to Arp2/3 complex regulating actin dynamics. It is known that recruitment into lamella promotes polymerization actin, although how it does this unclear. In study, we found PTP61F, Drosophila homolog mammalian PTP1B, can reverse colocalizes with in S2 cells. be translocalized cytosol cell membrane either increasing or reducing endogenous PTP61F. This reciprocal regulation also involved modulating level, which thought affect stability complex. Using mass spectrometry, identified several important tyrosine sites Abi. We compared translocalization half-life wild type (wt) phosphomutant their abilities restore lamellipodia structure Abi-reduced have reduced ability translocalize shorter than wt could fully structure, not. Together, these findings suggest PTP61F may regulate localization formation lamella.

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