Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für Biochemie     Collection: Independent Junior Research Groups     Display Documents



ID: 29180.0, MPI für Biochemie / Independent Junior Research Groups
Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis
Authors:Lane, J. D.; Lucocq, J.; Pryde, J.; Barr, F.; Woodman, P. G.; Allan, V. J.; Lowe, M.
Language:English
Date of Publication (YYYY-MM-DD):2002-02-04
Title of Journal:Journal of Cell Biology
Journal Abbrev.:J. Cell Biol.
Volume:156
Issue / Number:3
Start Page:495
End Page:509
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:The mammalian Golgi complex is comprised of a ribbon of stacked cisternal membranes often located in the pericentriolar region of the cell. Here, we report that during apoptosis the Golgi ribbon is fragmented into dispersed clusters of tubulo- vesicular membranes. We have found that fragmentation is caspase dependent and identified GRASP65 (Golgi reassembly and stacking protein of 65 kD) as a novel caspase substrate. GRASP65 is cleaved specifically by caspase-3 at conserved sites in its membrane distal COOH terminus at an early stage of the execution phase. Expression of a caspase-resistant form of GRASP65 partially preserved cisternal stacking and inhibited breakdown of the Golgi ribbon in apoptotic cells. Our results suggest that GRASP65 is an important structural component required for maintenance of Golgi apparatus integrity.
Free Keywords:Golgi apparatus; apoptosis; GRASP65; Golgi structure; caspase
Comment of the Author/Creator:Date: 2002, FEB 4
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Independent Junior Research Groups/Intracellular Protein Transport (F. Barr)
External Affiliations:Univ Manchester, Sch Biol Sci, 2-205 Stopford Bldg,Oxford Rd,; Manchester M13 9PT, Lancs, England; Univ Manchester, Sch Biol Sci, Manchester M13 9PT, Lancs, England; Univ Dundee, Sch Life Sci, Dundee DD1 5EH, Scotland; Univ Edinburgh, Dept Med & Radiol Sci, Edinburgh EH8 9YL, Midlothian, Scotland
Identifiers:ISI:000176425500008 [ID No:1]
ISSN:0021-9525 [ID No:2]
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.