A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold MP1 on a late endosomal/lysosomal compartment

Wunderlich, Winfried, Fialka, Irene, Teis, David, Alpi, Arno, Pfeifer, Andrea, Parton, Robert G., Lottspeich, Friedrich and Huber, Lukas A. (2001) A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold MP1 on a late endosomal/lysosomal compartment. Journal of Cell Biology, 152 4: 765-776. doi:10.1083/jcb.152.4.765

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Author Wunderlich, Winfried
Fialka, Irene
Teis, David
Alpi, Arno
Pfeifer, Andrea
Parton, Robert G.
Lottspeich, Friedrich
Huber, Lukas A.
Title A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold MP1 on a late endosomal/lysosomal compartment
Journal name Journal of Cell Biology   Check publisher's open access policy
ISSN 0021-9525
1540-8140
Publication date 2001-02-01
Year available 2001
Sub-type Article (original research)
DOI 10.1083/jcb.152.4.765
Open Access Status File (Publisher version)
Volume 152
Issue 4
Start page 765
End page 776
Total pages 12
Editor I. Mellman
M. Rossner
Place of publication New York, NY, United States
Publisher The Rockefeller University Press
Language eng
Abstract We have identified a novel, highly conserved protein of 14 kD copurifying with late endosomes/lysosomes on density gradients. The protein, now termed p14, is peripherally associated with the cytoplasmic face of late endosomes/lysosomes in a variety of different cell types. In a two-hybrid screen with p14 as a bait, we identified the mitogen-activated protein kinase (MAPK) scaffolding protein MAPK/extracellular signal-regulated kinase (ERK) kinase (MEK) partner 1 (MP1) as an interacting protein. We confirmed the specificity of this interaction in vitro by glutathione S-transferase pull-down assays and by coimmunoprecipitation, cosedimentation on glycerol gradients, and colocalization. Moreover, expression of a plasma membrane-targeted p14 causes mislocalization of coexpressed MP1. In addition, we could reconstitute protein complexes containing the p14-MP1 complex associated with ERK and MEK in vitro. The interaction between p14 and MP1 suggests a MAPK scaffolding activity localized to the cytoplasmic surface of late endosomes/lysosomes, thereby combining catalytic scaffolding and subcellular compartmentalization as means to modulate MAPK signaling within a cell.
Keyword Cell Biology
Signal Transduction Scaffold
Mek
Erk
Subcellular Localization
Endocytosis
Epidermal Growth-factor
2-dimensional Gel-electrophoresis
Signal-transduction
Epithelial-cells
Factor Receptor
Map-kinase
Subcellular Fractionation
Endosomes
Pathways
Q-Index Code C1
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Wed, 15 Aug 2007, 02:58:15 EST