A novel hook-related protein family and the characterization of Hook-related protein 1

Simpson, Fiona, Martin, Sally, Evans, Timothy M., Kerr, Markus, James, David E., Parton, Robert G., Teasdale, Rohan D. and Wicking, Carol (2005) A novel hook-related protein family and the characterization of Hook-related protein 1. Traffic, 6 6: 442-458. doi:10.1111/j.1600-0854.2005.00289.x


Author Simpson, Fiona
Martin, Sally
Evans, Timothy M.
Kerr, Markus
James, David E.
Parton, Robert G.
Teasdale, Rohan D.
Wicking, Carol
Title A novel hook-related protein family and the characterization of Hook-related protein 1
Journal name Traffic   Check publisher's open access policy
ISSN 1398-9219
1600-0854
Publication date 2005-06-01
Sub-type Article (original research)
DOI 10.1111/j.1600-0854.2005.00289.x
Volume 6
Issue 6
Start page 442
End page 458
Total pages 17
Place of publication Koebenhavn, Denmark
Publisher Blackwell Munksgaard
Language eng
Subject C1
270199 Biochemistry and Cell Biology not elsewhere classified
780105 Biological sciences
0601 Biochemistry and Cell Biology
Formatted abstract
The spatial organization of organelles within a cell is dependent on microtubules. Recently, members of the Hook family of proteins have been proposed to function in linking organelles to microtubules. We report the identification of a completely novel protein family, the Hook-related protein (HkRP) family, from which the Hook proteins have diverged. Bioinformatic analysis of the HkRP family revealed several conserved domains, including a unique C-terminal HkRP domain. The central region of each protein is comprised of an extensive coiled-coil domain, and the N-terminus contains a putative microtubule-binding domain. This domain has been shown to bind microtubules in the Hook protein and show that the HkRP1 protein is microtubule-associated. While endogenous HkRP1 has no distinct organelle association, expression of the C-terminal membrane-binding domain suggests a function of the HkRP1 in early endosome. Ultrastructural studies reveal that expression of the C-terminal HkRP1 domain causes an accumulation of internal membranes with an electron-dense coat. Co-localization studies show a concomitant redistribution of the early endosome marker sorting-nexin 1 but not the early endosome antigen-1 (EEA1). The steady-state distribution of the epidermal growth factor receptor is also specifically disrupted by expression of the C-terminal domain. We propose that HkRP1 is involved in the process of tubulation of sorting nexin-1 positive membranes from early endosome subdomains.
Copyright © Blackwell Munksgaard 2005
Keyword Cell Biology
Hook Protein
Kiaa1212
Membrane Trafficking
Microtubule
Vesicles
Growth-factor Receptor
Sorting Nexin-1
Endocytic Trafficking
Dynactin Complex
Endosomes
Drosophila
Transport
Binding
Microtubules
Degradation
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 16:10:41 EST