NDLI: Protein kinase C spatially and temporally regulates gap junctional communication during human wound repair via phosphorylation of connexin43 on serine368

Content Provider	PubMed Central
Author	Richards, Theresa S. Dunn, Clarence A. Carter, William G. Usui, Marcia L. Olerud, John E. Lampe, Paul D.
Abstract	Phosphorylation of connexin43 (Cx43) on serine368 (S368) has been shown to decrease gap junctional communication via a reduction in unitary channel conductance. Examination of phosphoserine368 (pS368) in normal human skin tissue using a phosphorylation site–specific antibody showed relatively even distribution throughout the epidermal layers. However, 24 h after wounding, but not at 6 or 72 h, pS368 levels were dramatically increased in basal keratinocytes and essentially lost from suprabasal layers adjacent to the wound (i.e., within 200 μm of it). Scratch wounding of primary human keratinocytes caused a protein kinase C (PKC)-dependent increase in pS368 in cells adjacent to the scratch, with a time course similar to that found in the wounds. Keratinocytes at the edge of the scratch also transferred dye much less efficiently at 24 h, in a manner dependent on PKC. However, keratinocyte migration to fill the scratch required early (within <6 h) gap junctional communication. Our evidence indicates that PKC-dependent phosphorylation of Cx43 at S368 creates dynamic communication compartments that can temporally and spatially regulate wound healing.
Related Links	http://dx.doi.org/10.1083/jcb.200404142
Ending Page	562
Page Count	8
Starting Page	555
File Format	PDF
ISSN	00219525
e-ISSN	15408140
Journal	The Journal of Cell Biology
Issue Number	3
Volume Number	167
Language	English
Publisher	The Rockefeller University Press
Publisher Date	2004-11-08
Access Restriction	Open
Rights Holder	The Rockefeller University Press
Subject Keyword	Cell Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine

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Protein kinase C spatially and temporally regulates gap junctional communication during human wound repair via phosphorylation of connexin43 on serine368

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