| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Oh, Seung Hyun Choi, Youngsok Lee, Ok-hee Songyang, Zhou Kang, Ju-hee Lee, Jinkyoung Yoon, Ho-geun Lee, Keun Ho Woo, Yun Mi Bae, Soo-kyung |
| Description |
Author Affiliation: Lee OH ( Department of Biomedical Science, CHA University, Seongnam-si, Gyeonggi-do, Republic of Korea); Lee J ( Severance Integrative Research Institute for Cerebral and Cardiovascular Diseases, Yonsei University Health System, Seoul, Republic of Korea.); Lee KH ( Severance Integrative Research Institute for Cerebral and Cardiovascular Diseases, Yonsei University Health System, Seoul, Republic of Korea.); Woo YM ( Department of Biomedical Science, CHA University, Seongnam-si, Gyeonggi-do, Republic of Korea); Kang JH ( Research Institute, National Cancer Center, Goyang-si, Gyeonggi-do, Republic of Korea); Yoon HG ( Department of Biochemistry and Molecular Biology, Center for Chronic Metabolic Disease Research, Yonsei University College of Medicine, Seoul, Republic of Korea.); Bae SK ( Department of Dental Pharmacology, School of Dentistry, Pusan National University, Yangsan, Republic of Korea.); Songyang Z ( Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.); Oh SH ( Research Institute, National Cancer Center, Goyang-si, Gyeonggi-do, Republic of Korea); Choi Y ( Department of Biomedical Science, CHA University, Seongnam-si, Gyeonggi-do, Republic of Korea. Electronic address: youngsokchoi@cha.ac.kr.) |
| Abstract |
The tripartite motif containing (TRIM) proteins are a large family of proteins that have been implicated in many biological processes including cell differentiation, apoptosis, transcriptional regulation, and signaling pathways. Here, we show that TRIM15 co-localized to focal adhesions through homo-dimerization and significantly suppressed cell migration. Domain mapping analysis indicated that B-box2 and PRY domains were essential for TRIM15 localization to focal adhesions and inhibition of cell migration. Our protein-protein interaction screen of TRIM15 with the integrin adhesome identified several TRIM15 interacting proteins including coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. TRIM15 expression was tissue-restricted and downregulated in colon cancer. Level of TRIM15 expression was associated with colon cancer cell migration, as well as both in vitro and in vivo tumor growth. These data provide novel insights into the role of TRIM15 as an additional component of the integrin adhesome, regulating cell migration, and suggest that TRIM15 may function as a tumor suppressor of colon cancer. |
| ISSN |
00063002 |
| Journal |
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number |
2 |
| Volume Number |
1853 |
| Language |
English |
| Publisher |
Elsevier |
| Publisher Date |
2015-02-01 |
| Publisher Place |
Netherlands |
| Access Restriction |
Open |
| Subject Keyword |
Carcinogenesis Genetics Pathology Colonic Neoplasms DNA-Binding Proteins Metabolism Focal Adhesions Actins Adenocarcinoma Animals Cell Adhesion Cell Line, Tumor Cell Movement Cell Proliferation Cortactin Chemistry Down-Regulation Epithelial Cells Extracellular Matrix Gene Expression Profiling Gene Expression Regulation, Neoplastic Mice, Nude Phosphorylation Protein Binding Protein Multimerization Protein Structure, Tertiary Protein Transport Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry |
| Content Type |
Text |
| Resource Type |
Article |
