Absence of a Human DnaJ Protein hTid-1(S) Correlates with Aberrant Actin Cytoskeleton Organization in Lesional Psoriatic Skinopen access
- Authors
- Choi, Ji Hye; Choi, Dae-Kyoung; Sohn, Kyung-Cheol; Kwak, Sang Su; Suk, Jinkyu; Lim, Jong-Soon; Shin, Incheol; Kim, Sung-Woo; Lee, Jeung-Hoon; Joe, Cheol O.
- Issue Date
- Jul-2012
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY, v.287, no.31, pp.25954 - 25963
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Volume
- 287
- Number
- 31
- Start Page
- 25954
- End Page
- 25963
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/165202
- DOI
- 10.1074/jbc.M111.313809
- ISSN
- 0021-9258
- 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.
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