Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis

Lowe, M., Rabouille, C., Nakamura, N., Watson, R., Jackman, M., Jamsa, E., Rahman, D., Pappin, D. J., Warren, G. (1998) Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis. Cell, 94 (6). pp. 783-93. ISSN 0092-8674 (Print)0092-8674 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/9753325
DOI: 10.1016/S0092-8674(00)81737-7

Abstract

Mitotic fragmentation of the Golgi apparatus can be largely explained by disruption of the interaction between GM130 and the vesicle-docking protein p115. Here we identify a single serine (Ser-25) in GM130 as the key phosphorylated target and Cdc2 as the responsible kinase. MEK1, a component of the MAP kinase signaling pathway recently implicated in mitotic Golgi fragmentation, was not required for GM130 phosphorylation or mitotic fragmentation either in vitro or in vivo. We propose that Cdc2 is directly involved in mitotic Golgi fragmentation and that signaling via MEK1 is not required for this process.

Item Type: Paper
Additional Information: Lowe, M Rabouille, C Nakamura, N Watson, R Jackman, M Jamsa, E Rahman, D Pappin, D J Warren, G Wellcome Trust/United Kingdom Research Support, Non-U.S. Gov't United states Cell Cell. 1998 Sep 18;94(6):783-93.
Uncontrolled Keywords: Autoantigens CDC2 Protein Kinase/ metabolism Golgi Apparatus/chemistry/ enzymology Guanine Nucleotide Exchange Factors HeLa Cells Humans MAP Kinase Kinase 1 Membrane Proteins/ metabolism Mitogen-Activated Protein Kinase Kinases Mitosis/ physiology Molecular Sequence Data Phosphorylation Protein Binding/physiology Protein-Serine-Threonine Kinases/metabolism Protein-Tyrosine Kinases/metabolism Proteins/metabolism Sequence Homology, Amino Acid Serine/metabolism
Subjects: organs, tissues, organelles, cell types and functions > organelles, types and functions > golgi
organs, tissues, organelles, cell types and functions > organelles, types and functions > mitosis
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > Protein kinase C
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Kathleen Darby
Date: 18 September 1998
Date Deposited: 01 May 2014 16:47
Last Modified: 01 May 2014 16:47
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29910

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