Absence of a Human DnaJ Protein hTid-1(S) Correlates with Aberrant Actin Cytoskeleton Organization in Lesional Psoriatic Skin

Title
Absence of a Human DnaJ Protein hTid-1(S) Correlates with Aberrant Actin Cytoskeleton Organization in Lesional Psoriatic Skin
Author
신인철
Keywords
Cell Migration; Cytoskeleton; Keratinocytes; p38 MAPK; Psoriasis; F-actin; HSP27; MK5; Epidermis; hTid-1
Issue Date
2012-07
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
Journal of Biological Chemistry, 2012, 287(31), P.25954~26017
Abstract
The biochemical mechanism by which the human tumorous imaginal disc1(S) (hTid-1(S)) interferes with actin cytoskeleton organization in keratinocytes of human skin epidermis was investigated. We found that hTid-1, specifically hTid-1(S), interacts with MK5, a p38-regulated/activated protein kinase, and inhibits the protein kinase activity of MK5 that phosphorylates heat shock protein HSP27 in cultured HeLa cells. Thus, hTid-1(S) expression inhibits the phosphorylation of HSP27 known to play important roles in F-actin polymerization and actin cytoskeleton organization. The interplay between MK5/HSP27 signaling and hTid-1(S) expression was supported by the inhibition of HSP27 phosphorylation and MK5 activity in HeLa cells in response to hypoxia during which hTid-1(S) expression was down-regulated. We also found that overexpression of hTid-1(S) results in the inhibition of HSP27 phosphorylation, F-actin polymerization, and actin cytoskeleton organization in transduced HaCaT keratinocytes. This study further proposes that the loss of hTid-1(S) expression in the basal layer of skin epidermis correlates with the enhanced HSP27 phosphorylation, keratinocyte hyperproliferation, and excess actin cytoskeleton organization in lesional psoriatic skin.
URI
http://www.jbc.org/content/287/31/25954.fullhttp://hdl.handle.net/20.500.11754/66113
ISSN
0021-9258
DOI
10.1074/jbc.M111.313809
Appears in Collections:
COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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