- 【Updated on May 12, 2025】 Integration of CiNii Dissertations and CiNii Books into CiNii Research
- Trial version of CiNii Research Knowledge Graph Search feature is available on CiNii Labs
- Suspension and deletion of data provided by Nikkei BP
- Regarding the recording of “Research Data” and “Evidence Data”
Heterogeneous Nuclear Ribonucleoprotein K Interacts with and Is Proteolyzed by Calpain in vivo
-
- KIMURA Eiichi
- <i>Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo</i>
-
- ABE Keiko
- <i>Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo</i>
-
- SUZUKI Koichi
- <i>Tokyo Metropolitan Institute of Gerontology</i>
-
- SORIMACHI Hiroyuki
- <i>Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo</i> <i>CREST, JST</i>
Bibliographic Information
- Other Title
-
- Heterogeneous Nuclear Ribonucleoprotein K Interacts with and Is Proteolyzed by Calpain<i>in vivo</i>
Search this article
Description
Calpain is a cytosolic “modulator protease” that modulates cellular functions in response to Ca2+. To identify in vivo substrates of calpain, yeast two-hybrid screening was done using the 5-EF-hand (penta-EF-hand; PEF) domain of the μ-calpain large subunit (domain IV), since several possible in vivo substrates for calpain have been previously reported to bind to the 5-EF-hand domains. Other than the regulatory subunit of calpain, which binds to the domain IV, heterogeneous nuclear ribonucleoproteins (hnRNP) K and R were identified, and shown to be proteolyzed by μ-calpain in vitro. When expressed in COS7 cells, hnRNP K and μ-calpain co-localized in the cytosol, and Ca2+-ionophore stimulation of the cells resulted in proteolysis of hnRNP K, indicating that hnRNP K is an in vivo substrate for calpain. Now, hnRNP K is considered to function as a scaffold protein for its binding proteins, such as PKCδ and C/EBPβ, which were reported to be calpain substrates, suggesting that hnRNP-K is a scaffold for calpain to proteolyze these proteins.<br>
Journal
-
- Bioscience, Biotechnology, and Biochemistry
-
Bioscience, Biotechnology, and Biochemistry 67 (8), 1786-1796, 2003
Japan Society for Bioscience, Biotechnology, and Agrochemistry
- Tweet
Keywords
Details 詳細情報について
-
- CRID
- 1390282681452151808
-
- NII Article ID
- 110002694302
-
- NII Book ID
- AA10824164
-
- COI
- 1:CAS:528:DC%2BD3sXnt1Wmsrg%3D
-
- ISSN
- 13476947
- 09168451
-
- NDL BIB ID
- 6665729
-
- PubMed
- 12951515
-
- Text Lang
- en
-
- Article Type
- journal article
-
- Data Source
-
- JaLC
- NDL Search
- Crossref
- PubMed
- CiNii Articles
- OpenAIRE
-
- Abstract License Flag
- Disallowed