NHERF1 regulates actin cytoskeleton organization through modulation of  -actinin-4 stability

Sun, L., Zheng, J., Wang, Q., Song, R., Liu, H., Meng, R., Tao, T., Si, Y., Jiang, Wen Guo ORCID: https://orcid.org/0000-0002-3283-1111 and He, J. 2016. NHERF1 regulates actin cytoskeleton organization through modulation of  -actinin-4 stability. The FASEB Journal 30 (2) , pp. 578-589. 10.1096/fj.15-275586

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Abstract

The actin cytoskeleton is composed of a highly dynamic network of filamentous proteins, yet the molecular mechanism that regulates its organization and remodeling remains elusive. In this study, Na+/H+ exchanger regulatory factor (NHERF)-1 loss-of-function and gain-of-function experiments reveal that polymerized actin cytoskeleton (F-actin) in HeLa cells is disorganized by NHERF1, whereas actin protein expression levels exhibit no detectable change. To elucidate the molecular mechanism underlying actin cytoskeleton disorganization by NHERF1, a combined 2-dimensional electrophoresis–matrix-assisted laser desorption/ionization–time of flight mass spectrometry approach was used to screen for proteins regulated by NHERF1 in HeLa cells. α-Actinin-4, an actin cross-linking protein, was identified. Glutathione S-transferase pull-down and coimmunoprecipitation studies showed the α-actinin-4 carboxyl-terminal region specifically interacted with the NHERF1 postsynaptic density 95/disc-large/zona occludens-1 domain. The NHERF1/α-actinin-4 interaction increased α-actinin-4 ubiquitination and decreased its expression levels, resulting in actin cytoskeleton disassembly. Our study identified α-actinin-4 as a novel NHERF1 interaction partner and provided new insights into the regulatory mechanism of the actin cytoskeleton by NHERF1.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine
Subjects:	R Medicine > R Medicine (General)
Publisher:	Federation of American Society of Experimental Biology
ISSN:	0892-6638
Date of Acceptance:	21 September 2015
Last Modified:	28 Oct 2022 10:29
URI:	https://orca.cardiff.ac.uk/id/eprint/78535

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