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Int. J. Mol. Sci. 2016, 17(9), 1401; doi:10.3390/ijms17091401

Multifaceted Roles of ALG-2 in Ca2+-Regulated Membrane Trafficking

Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
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Author to whom correspondence should be addressed.
Academic Editor: Charles J. Malemud
Received: 21 July 2016 / Revised: 18 August 2016 / Accepted: 19 August 2016 / Published: 26 August 2016
(This article belongs to the Special Issue Metalloproteins 2017)
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Abstract

ALG-2 (gene name: PDCD6) is a penta-EF-hand Ca2+-binding protein and interacts with a variety of proteins in a Ca2+-dependent fashion. ALG-2 recognizes different types of identified motifs in Pro-rich regions by using different hydrophobic pockets, but other unknown modes of binding are also used for non-Pro-rich proteins. Most ALG-2-interacting proteins associate directly or indirectly with the plasma membrane or organelle membranes involving the endosomal sorting complex required for transport (ESCRT) system, coat protein complex II (COPII)-dependent ER-to-Golgi vesicular transport, and signal transduction from membrane receptors to downstream players. Binding of ALG-2 to targets may induce conformational change of the proteins. The ALG-2 dimer may also function as a Ca2+-dependent adaptor to bridge different partners and connect the subnetwork of interacting proteins. View Full-Text
Keywords: ALG-2; ALIX; calcium; COPII; ESCRT; membrane repair; multivesicular body; PDCD6; protein–protein interaction; Sec31A ALG-2; ALIX; calcium; COPII; ESCRT; membrane repair; multivesicular body; PDCD6; protein–protein interaction; Sec31A
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Maki, M.; Takahara, T.; Shibata, H. Multifaceted Roles of ALG-2 in Ca2+-Regulated Membrane Trafficking. Int. J. Mol. Sci. 2016, 17, 1401.

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