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A likely role for the PH-domain containing protein, PEPP2/ PLEKHA5, at the membrane-microtubule cytoskeleton interface

Yi ZOU1*, Timothy C COX2
School of Molecular Biosciences, University of Adelaide, Adelaide, South Australia and Department of Anatomy & Developmental Biology, Monash University, Clayton, Victoria, Australia
* Current address:
1 Department of Biology, School of Life Science and Technology, Jinan University, Guangzhou, China; and
2 Department of Pediatrics (Craniofacial Medicine), University of Washington; Center for Developmental Biology & Regenerative Medicine, Seattle Children's Research Institute; Seattle, WA, USA 98101
Corresponding author: Timothy C Cox, tccox@u.washington.edu

BIOCELL 2013, 37(3), 55-61. https://doi.org/10.32604/biocell.2013.37.055

Abstract

PH (pleckstrin homology) domains are well known to bind membrane phosphoinositides with different specificities and direct PH domain-containing proteins to discrete subcellular compartments with assistances of alternative binding partners. PH domain-containing proteins have been found to be involved in a wide range of cellular events, including signalling, cytoskeleton rearrangement and vesicular trafficking. Here we showed that a novel PH domain-containing protein, PEPP2 (also known as PLEKHA5), displays moderate phosphoinositide binding specificity. Full length PEPP2 was observed to variably associate with both the plasma membrane and microtubules. The membrane-associated PEPP2 nucleated at cell-cell contacts and the leading edge of migrating cells. Overexpression of PEPP2 increased membrane microviscosity, indicating a potential role for PEPP2 in regulating function of microtubule-dependent membrane functions.

Keywords

Microtubule, membrane, phosphoinositide, microviscosity, PH domain

Cite This Article

ZOU, Y., COX, T. C. (2013). A likely role for the PH-domain containing protein, PEPP2/ PLEKHA5, at the membrane-microtubule cytoskeleton interface. BIOCELL, 37(3), 55–61.

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This work is licensed under a Creative Commons Attribution 4.0 International License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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