The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain

Seemann, Joachim, Weber, Klaus, Osborn, Mary, Parton, Robert G. and Gerke, Volker (1996) The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain. Molecular Biology of the Cell, 7 9: 1359-1374. doi:10.1091/mbc.7.9.1359

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ249165_OA.pdf Full text (open access) application/pdf 5.20MB 0

Author Seemann, Joachim
Weber, Klaus
Osborn, Mary
Parton, Robert G.
Gerke, Volker
Title The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain
Formatted title
The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 1996-09
Sub-type Article (original research)
DOI 10.1091/mbc.7.9.1359
Open Access Status File (Publisher version)
Volume 7
Issue 9
Start page 1359
End page 1374
Total pages 16
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Language eng
Formatted abstract
Annexin I is a member of a multigene family of Ca2+/phospholipid- binding proteins and a major substrate for the epidermal growth factor (EGF) receptor kinase, which has been implicated in membrane-related events along the endocytotic pathway, in particular in the sorting of internalized EGF receptors occurring in the multivesicular body. We analyzed in detail the intracellular distribution of this annexin by cell fractionation and immunoelectron microscopy. These studies used polyclonal as well as a set of species-specific monoclonal antibodies, whose epitopes were mapped to the lateral surface of the molecule next to a region thought to be involved in vesicle aggregation. Unexpectedly, the majority of annexin I was identified on early and not on multivesicular endosomes in a form that required micromolar levels of Ca2+ for the association. The specific cofractionation with early endosomes was also observed in transfected baby hamster kidney cells when the intracellular fate of ectopically expressed porcine annexin I was analyzed by using the species-specific monoclonal antibodies in Western blots of subcellular fractions. Interestingly, a truncation of the N-terminal 26, but not the N-terminal 13 residues of annexin I altered its intracellular distribution, shifting it from fractions containing early to those containing late and multivesicular endosomes. These findings underscore the regulatory importance of the N-terminal domain and provide evidence for an involvement of annexin I in early endocytotic processes.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 62 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Fri, 09 Sep 2011, 20:33:52 EST by System User on behalf of Learning and Research Services (UQ Library)