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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
2000-11-20
pubmed:abstractText
Cytoplasmic dynein is a molecular motor complex consisting of four major classes of polypeptide: the catalytic heavy chains (HC), intermediate chains (IC), light intermediate chains (LIC), and light chains (LC). Previous studies have reported that the ICs bind near the N terminus of the HCs, which is thought to correspond to the base of the dynein complex. In this study, we co-overexpressed cytoplasmic dynein subunits in COS-7 cells to map HC binding sites for the ICs and LICs, as well as HC dimerization. We have found that the LICs bind directly to the N terminus of the HC, adjacent to and overlapping with the IC binding site, consistent with a role for the LICs in cargo binding. Mutation of the LIC P-loop had no detectable effect on HC binding. We detected no direct interaction between the ICs and LICs. Using triple overexpression of HC, IC and LIC, we found that both IC and LIC are present in the same complexes, a result verified by anti-IC immunoprecipitation of endogenous complexes and immunoblotting. Our results indicate that the LICs and ICs must be located on independent surfaces of cytoplasmic dynein to allow each to interact with other proteins without steric interference.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32769-74
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding.
pubmed:affiliation
Department of Cell Biology, University of Massachusetts Medical Center, Worcester, Massachusetts 01605, USA.
pubmed:publicationType
Journal Article