JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online 20 February 2001. doi:10.1083/jcb.152.4.765
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 940K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wunderlich, W.
Right arrow Articles by Huber, L. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wunderlich, W.
Right arrow Articles by Huber, L. A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
© The Rockefeller University Press, 0021-9525/2001/2/765/ $5.00
The Journal of Cell Biology, Volume 152, Number 4, February 19, 2001 765-776


Original Article

A Novel 14-Kilodalton Protein Interacts with the Mitogen-activated Protein Kinase Scaffold MP1 on a Late Endosomal/Lysosomal Compartment

Winfried Wunderlicha, Irene Fialkaa, David Teisa, Arno Alpia, Andrea Pfeifera, Robert G. Partonb, Friedrich Lottspeichc, and Lukas A. Hubera
a Research Institute of Molecular Pathology, A-1030 Vienna, Austria
b Institute for Molecular Bioscience, Centre for Microscopy and Microanalysis, and Department of Physiology and Pharmacology, University of Queensland, Queensland 4072, Brisbane, Australia
c Max-Planck-Institute of Biochemistry, D-82152 Martinsried, Germany

Correspondence to: Lukas A. Huber, Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria. Tel:43-179-730-885 Fax:43-179-87-153 E-mail:huber{at}nt.imp.univie.ac.at.

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.

Key Words: signal transduction scaffold, MEK, ERK, subcellular localization, endocytosis


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents