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

Yi Zou, Timothy C. Cox

Research output: Contribution to journalArticleResearchpeer-review

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)55-61
Number of pages7
JournalBiocell
Volume37
Issue number3
Publication statusPublished - 2013

Keywords

  • Membrane
  • Microtubule
  • Microviscosity
  • PH domain
  • Phosphoinositide

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