Osteoactivin is a type I transmembrane protein upregulated by unloading stresses, including denervation, prolonged bed rest, and space flight, but the regulatory mechanisms of its expression and activation under these conditions remain undefined. Here we report that osteoactivin protein exists in two forms: an intact transmembrane form and a secreted form. The secreted form, the extracellular fragment of osteoactivin, was produced by ectodomain shedding and was released into a culture medium. Amino acid sequence analysis of the carboxy-terminal fragment of osteoactivin (OA-CTF) revealed that cleavage of osteoactivin by proteases occurred both at the cell surface and within the cell membrane. Localization analysis demonstrated translocalization of OA-CTF to the nucleus and the endoplasmic reticulum. Moreover, RNA binding proteins, which regulate pre-mRNA splicing, were identified as OA-CTF binding proteins. These results suggest that OA-CTF formed by ectodomain shedding is involved in the regulation of pre-mRNA splicing.
Bioscience, Biotechnology, and Biochemistry
Volume 76, 2012 - Issue 12
![Sample our Bioscience journals, sign in here to start your access, Latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5925/TOC-Subject-Sample-2021-Bioscience.jpg"})
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related Research Data
ADAM10 releases a soluble form of the GPNMB/Osteoactivin extracellular domain with angiogenic properties.
Source:
Public Library of Science (PLoS)
ADAM10, the Rate-limiting Protease of Regulated Intramembrane Proteolysis of Notch and Other Proteins, Is Processed by ADAMS-9, ADAMS-15, and the γ-Secretase *
Source:
American Society for Biochemistry & Molecular Biology (ASBMB)
Roles for SR Proteins and hnRNP A1 in the Regulation of c-src Exon N1
Source:
American Society for Microbiology
Regulation of Alternative Splicing of Protein Kinase Cβ by Insulin
Source:
Elsevier BV
Ectodomain Shedding and Regulated Intracellular Proteolysis in the Central Nervous System
Source:
Bentham Science Publishers Ltd.
A carboxy-terminal deletion mutant of protein kinase C beta II inhibits insulin-stimulated 2-deoxyglucose uptake in L6 rat skeletal muscle cells
Source:
The Endocrine Society
Osteoactivin upregulates expression of MMP-3 and MMP-9 in fibroblasts infiltrated into denervated skeletal muscle in mice
Source:
American Physiological Society
GPNMB Induces BiP Expression by Enhancing Splicing of BiP Pre-mRNA during the Endoplasmic Reticulum Stress Response
Source:
Nature Publishing Group
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Source:
Springer Science and Business Media LLC
Multiple roles of arginine/serine-rich splicing factors in RNA processing
Source:
Portland Press Ltd.
RS domains contact the pre-mRNA throughout spliceosome assembly.
Source:
Elsevier BV
Protein Ectodomain Shedding
Source:
American Chemical Society (ACS)
Structures of CSL, Notch and Mastermind proteins: piecing together an active transcription complex.
Source:
Elsevier BV
Linking provided by
