Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2009-7-16
pubmed:abstractText
How ciliary and flagellar motility is regulated is a challenging problem. The flagellar movement in Chlamydomonas reinhardtii is in part regulated by phosphorylation of a 138 kD intermediate chain (IC138) of inner arm dynein f (also called I1). In the present study, we found that the axoneme of mutants lacking dynein f lacks a novel protein having ankyrin repeat motifs, registered as FAP120 in the flagellar proteome database. FAP120 is also missing or decreased in the axonemes of bop5, a mutant that has a mutation in the structural gene of IC138 but assembles the dynein f complex. Intriguingly, the amounts of FAP120 in the axonemes of different alleles of bop5 and several dynein f-lacking mutants roughly parallel their contents of IC138. These results suggest a weak but stoichiometric interaction between FAP120 and IC138. We propose that FAP120 functions in the regulatoryprocess as part of a protein complex involving IC138. Cell Motil. Cytoskeleton 2008. (c) 2008 Wiley-Liss, Inc.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-10459015, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-10858448, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-11907279, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-12211628, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-12684385, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-1387404, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-1387971, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-14978211, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-15020587, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-15304520, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-15469982, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-15657081, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-15998802, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-17176038, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-17981992, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-1825085, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-269405, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-2714235, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-2974040, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-3224813, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-3821567, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-388439, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-4379719, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-6725408, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-7476482, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-7579690, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-8195292, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-9008711, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-9008712, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-9151671, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-9194178, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-9490726, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-9585416, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-9843573, http://linkedlifedata.com/resource/pubmed/commentcorrection/19021242-9843574
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1097-0169
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
448-56
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
A novel ankyrin-repeat protein interacts with the regulatory proteins of inner arm dynein f (I1) of Chlamydomonas reinhardtii.
pubmed:affiliation
Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan. kamiyar@biol.s.u-tokyo.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural