A large family of endosome-localized proteins related to sorting nexin 1

Teasdale, R. D., Loci, D., Houghton, F., Karlsson, L. and Gleeson, P. A. (2001) A large family of endosome-localized proteins related to sorting nexin 1. Biochemical Journal, 358 1: 7-16. doi:10.1042/0264-6021:3580007

Author Teasdale, R. D.
Loci, D.
Houghton, F.
Karlsson, L.
Gleeson, P. A.
Title A large family of endosome-localized proteins related to sorting nexin 1
Journal name Biochemical Journal   Check publisher's open access policy
ISSN 0264-6021
Publication date 2001-08-15
Year available 2001
Sub-type Article (original research)
DOI 10.1042/0264-6021:3580007
Open Access Status
Volume 358
Issue 1
Start page 7
End page 16
Total pages 10
Place of publication London
Publisher Portland Press
Language eng
Abstract Sorting nexin 1 (SNX1), a peripheral membrane protein, has previously been shown to regulate the cell-surface expression of the human epidermal growth factor receptor [Kurten, Cadena and Gill (1996) Science 272, 1008-1010]. Searches of human expressed sequence tag databases with SNX1 revealed eleven related human cDNA sequences, termed SNX2 to SNX12, eight of them novel. Analysis of SNX1-related sequences in the Saccharomyces cerevisiae genome clearly shows a greatly expanded SNX family in humans in comparison with yeast. On the basis of the predicted protein sequences, all members of this family of hydrophilic molecules contain a conserved 70 110-residue Phox homology (PX) domain, referred to as the SNX-PX domain. Within the SNX family, subgroups were identified on the basis of the Sequence similarities of the SNX-PX domain and the overall domain structure of each protein. The members of one subgroup, which includes human SNX1, SNX2, SNX4, SNX5 and SNX6 and the yeast Vps5p and YJL036W, all contain coiled-coil regions within their large C-terminal domains and are found distributed in both membrane and cytosolic fractions, typical of hydrophilic peripheral membrane proteins. Localization of the human SNX1 subgroup members in HeLa cells transfected with the full-length cDNA species revealed a similar intracellular distribution that in all cases overlapped substantially with the early endosome marker, early endosome autoantigen 1. The intracellular localization of deletion mutants and fusions with green fluorescent protein showed that the C-terminal regions of SNX1 and SNX5 are responsible for their endosomal localization. On the basis of these results, the functions of these SNX molecules are likely to be unique to endosomes, mediated in part by interactions with SNX-specific C-terminal sequences and membrane-associated determinants.
Keyword Biochemistry & Molecular Biology
membrane transport
protein sorting
receptor trafficking
Secondary Structure
Neural Networks
Sh3 Domains
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 101 times in Thomson Reuters Web of Science Article | Citations
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Created: Thu, 20 Sep 2007, 01:55:30 EST