Regulation of C1-Ten protein tyrosine phosphatase by p62/SQSTM1-mediated sequestration and degradation
SCIE
SCOPUS
- Title
- Regulation of C1-Ten protein tyrosine phosphatase by p62/SQSTM1-mediated sequestration and degradation
- Authors
- Koh, A; Park, D; Jeong, H; Lee, J; Lee, MN; Suh, PG; Ryu, SH
- Date Issued
- 2014-11
- Publisher
- CELLULAR SIGNALLING
- Abstract
- C1-Ten is a member of the tensin family of focal adhesion molecules but recent studies suggest it plays a more active role in many biological processes because of its potential association with diabetes and cancers. However, relatively little is known about the regulation of C1-Ten, such as changes in its protein level or cellular localization. The cellular localization of C1-Ten is Unique because it is expressed in cytoplasmic puncta but nothing is known about these puncta. Here, we show that p62 sequestrates C1-Ten into puncta, making C1-Ten diffuse into the cytoplasm upon p62 depletion. More importantly, p62-mediated C1-Ten sequestration promoted C1-Ten ubiquitination and proteasomal degradation. p62-mediated protein reduction was specific to C1-Ten, and not other tensins such as tensin1 and tensin3. Thus, our results link cellular localization of C1-Ten to an off-switch site for C1-Ten. Additionally, p62 expression increased but C1-Ten protein decreased during muscle differentiation, supporting a role for p62 as, a physiological regulator of C1-Ten. (C) 2014 Elsevier Inc. All rights reserved.
- Keywords
- C1-Ten; Tensin2; p62; Sequestosome; Degradation; SIGNAL-TRANSDUCTION; CELL-MIGRATION; NEGATIVE REGULATOR; SEQUESTOSOME 1/P62; SH2 DOMAIN; CANCER; P62; AUTOPHAGY; UBIQUITIN; BINDING
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/14256
- DOI
- 10.1016/J.CELLSIG.2014.07.033
- ISSN
- 0898-6568
- Article Type
- Article
- Citation
- CELLULAR SIGNALLING, vol. 26, no. 11, page. 2470 - 2480, 2014-11
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.