Pfister A, Hadjihannas M, Roehrig W, Schambony A, Behrens J (2012)
Publication Type: Journal article, Original article
Subtype: other
Publication year: 2012
Book Volume: 287
Pages Range: 35333-35340
Journal Issue: 42
EB1 is key factor in the organization of the microtubule cytoskeleton by binding to the plus-ends of microtubules and serving as a platform for a number of interacting proteins (termed +TIPs) that control microtubule dynamics. Together with its direct binding partner adenomatous polyposis coli (APC), EB1 can stabilize microtubules. Here, we show that Amer2 (APC membrane recruitment 2), a previously identified membrane-associated APC-binding protein, is a direct interaction partner of EB1 and acts as regulator of microtubule stability together with EB1. Amer2 binds to EB1 via specific (S/T)xIP motifs and recruits it to the plasma membrane. Coexpression of Amer2 and EB1 generates stabilized microtubules at the plasma membrane, whereas knockdown of Amer2 leads to destabilization of microtubules. Knockdown of Amer2, APC, or EB1 reduces cell migration, and morpholino-mediated down-regulation of Xenopus Amer2 blocks convergent extension cell movements, suggesting that the Amer2-EB1-APC complex regulates cell migration by altering microtubule stability.
APA:
Pfister, A., Hadjihannas, M., Roehrig, W., Schambony, A., & Behrens, J. (2012). Amer2 protein interacts with EB1 protein and adenomatous polyposis coli (APC) and controls microtubule stability and cell migration. Journal of Biological Chemistry, 287(42), 35333-35340. https://doi.org/10.1074/jbc.M112.385393
MLA:
Pfister, Astrid, et al. "Amer2 protein interacts with EB1 protein and adenomatous polyposis coli (APC) and controls microtubule stability and cell migration." Journal of Biological Chemistry 287.42 (2012): 35333-35340.
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