Publication: Scratching the surface: Actin’ and other roles for the C-terminal Eps15 homology domain protein, EHD2
Authors
Simone, Laura C. ; Naslavsky, Naava ; Caplan, Steve
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Publisher
F. Hernández y Juan F. Madrid. Universidad de Murcia. Departamento de Biología Celular e Histología
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DOI
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info:eu-repo/semantics/article
Description
Abstract
The C-terminal Eps15 homology domaincontaining
(EHD) proteins participate in multiple aspects
of endocytic membrane trafficking. Of the four
mammalian EHD proteins, EHD2 appears to be the most
disparate, both in terms of sequence homology, and in
subcellular localization/function. Since its initial
description as a plasma membrane-associated protein,
the precise function of EHD2 has remained enigmatic.
Various reports have suggested roles for EHD2 at the
plasma membrane, within the endocytic transport
system, and even in the nucleus. For example, EHD2
facilitates membrane fusion/repair in muscle cells.
Recently the focus has shifted to the role of EHD2 in
regulating caveolae. Indeed, EHD2 is highly expressed
in tissues rich in caveolae, including fat, muscle and
blood vessels. This review highlights cumulative
evidence linking EHD2 to actin-rich structures at the
plasma membrane, where the plasma membraneassociated
phospholipid phosphatidylinositol 4,5-
bisphosphate controls EHD2 recruitment. Herein we
examine the key pathways where EHD2 might function,
and address its potential involvement in these processes.
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Citation
Histology and Histopathology, vol. 29, nº 3 (2014)
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