Abstrakt interacts with and regulates the expression of sorting nexin-2.

作者: Mohammad Abdul-Ghani , Kristin L. Hartman , Johnny K. Ngsee

DOI: 10.1002/JCP.20285

关键词:

摘要: Cells maintain complex regulatory mechanisms to ensure temporal and spatial specificity of vesicular trafficking coordinate events within the various intracellular compartments with that other cellular processes. This requires sorting targeting proteins appropriate compartments. In yeast, vacuolar protein (VPS) family genes are involved in aspects vacuole biogenesis (Conibear Stevens, 1998; Sato et al., 2001; Katzmann 2002). One member this family, VPS5, is required for proper localization loss function resulting misdirection cell surface (Horazdovsky 1997; Seaman 1998). VPS5 belongs a collectively known as nexins (SNX), which human genome contains at least 16 homologues. Vps5p shows highest similarity mammalian SNX1, initially identified lysosomal degradation epidermal growth factor receptor (EGFR) (Kurten 1996). Thus, by directing EGFR degradative compartment, SNX1 could potentially alter duration signaling. effect on signaling implies levels SNX must be regulated optimal signal transduction. The characterized presence conserved phox homology (PX) domain, binds phosphatidylinositides (Xu Cozier 2002; Zhong contrast their lipid-binding abilities, role PX domains protein–protein interaction remains unclear. The C-terminal domain SNX2 Bin, amphiphysin, RVS (BAR) forms crescent-shaped dimer preferentially highly curved membranes (Peter 2003). Yeast “retromer” consisting four proteins: Vps17p, Vps26p, Vps29p, Vps35p (Seaman Seaman, 2004). appears conserved, orthologs these also exist large complexes (Haft 2000). Moreover, form sub-complex 1998, 2000), genetic analysis knockout mice indicates may have overlapping well unique functions (Schwarz Their ability subcomplexes provide basis functional overlap while formation heterogeneous provides diversity To identify might interact regulate SNX2, we initiated bacterial two-hybrid screen bait. We DEAD-box helicase, Abstrakt (Abs), an SNX2-interacting protein. showed N-terminal Abs interacts SNX2. Interestingly, both undergo nucleocytoplasmic shuttling, raising possibility can occur either compartment. altered serum withdrawal. Finally, co-expression wild type reduced expression unexpected novel mechanism whereby such RNA helicase Abs.

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