NDLI: Direct regulation of osteocytic connexin 43 hemichannels through AKT kinase activated by mechanical stimulation.

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Direct regulation of osteocytic connexin 43 hemichannels through AKT kinase activated by mechanical stimulation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kar, Rekha Batra, Nidhi Burra, Sirisha Gu, Sumin Jiang, Jean X. Riquelme, Manuel A.
Description	Author Affiliation: Batra N ( From the Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229-3900.)
Abstract	Connexin (Cx) 43 hemichannels in osteocytes are thought to play a critical role in releasing bone modulators in response to mechanical loading, a process important for bone formation and remodeling. However, the underlying mechanism that regulates the opening of mechanosensitive hemichannels is largely unknown. We have recently shown that Cx43 and integrin 5 interact directly with each other, and activation of PI3K appears to be required for Cx43 hemichannel opening by mechanical stimulation. Here, we show that mechanical loading through fluid flow shear stress (FFSS) increased the level of active AKT, a downstream effector of PI3K, which is correlated with the opening of hemichannels. Both Cx43 and integrin 5 are directly phosphorylated by AKT. Inhibition of AKT activation significantly reduced FFSS-induced opening of hemichannels and disrupted the interaction between Cx43 and integrin 5. Moreover, AKT phosphorylation on Cx43 and integrin 5 enhanced their interaction. In contrast to the C terminus of wild-type Cx43, overexpression of the C-terminal mutant containing S373A, a consensus site previously shown to be phosphorylated by AKT, failed to bind with 5 and hence could not inhibit hemichannel opening. Together, our results suggest that AKT activated by FFSS directly phosphorylates Cx43 and integrin 5, and Ser-373 of Cx43 plays a predominant role in mediating the interaction between these two proteins and Cx43 hemichannel opening, a crucial step to mediate the anabolic function of mechanical loading in the bone.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	15
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-04-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Connexin 43 Metabolism Gene Expression Regulation Integrin Alpha5 Osteocytes Proto-Oncogene Proteins C-akt Animals Cell Line Collagen Connexins Gap Junctions Mice Phosphorylation Protein Binding Protein Processing, Post-Translational Recombinant Fusion Proteins Serine Shear Strength Stress, Mechanical Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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