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J Proteomics. 2013 Jan 14;78:113-22. doi: 10.1016/j.jprot.2012.09.040. Epub 2012 Nov 10.

Proteomic analysis of the cilia membrane of Paramecium tetraurelia.

Author information

1
Department of Biology, University of Vermont, Burlington, VT 05405, USA. Electronic Junji.Yano@uvm.edu

Abstract

Channels, pumps, receptors, cyclases and other membrane proteins modulate the motility and sensory function of cilia, but these proteins are generally under-represented in proteomic analyses of cilia. Studies of these ciliary membrane proteins would benefit from a protocol to greatly enrich for integral and lipidated membrane proteins. We used LC-MS/MS to compare the proteomes of unfractionated cilia (C), the ciliary membrane (CM) and the ciliary membrane in the detergent phase (DP) of Triton X-114 phase separation. 55% of the proteins in DP were membrane proteins (i.e. predicted transmembrane or membrane-associated through lipid modifications) and 31% were transmembrane. This is to be compared to 23% membrane proteins with 9% transmembrane in CM and 9% membrane proteins with 3% transmembrane in C. 78% of the transmembrane proteins in the DP were found uniquely in DP, and not in C or CM. There were ion channels, cyclases, plasma membrane pumps, Ca(2+) dependent protein kinases, and Rab GTPases involved in the signal transduction in DP that were not identified in the other C and CM preparations. Of 267 proteins unique to the DP, 147 were novel, i.e. not found in other proteomic and genomic studies of cilia.

PMID:
23146917
PMCID:
PMC3667161
DOI:
10.1016/j.jprot.2012.09.040
[Indexed for MEDLINE]
Free PMC Article

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