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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
48
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pubmed:dateCreated |
1998-12-23
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pubmed:databankReference | |
pubmed:abstractText |
Kinectin, an integral membrane protein (160 kDa), was identified as a kinesin-binding protein. Analysis of the predicted amino acid sequence of kinectin cDNA indicated an alpha-helical coiled-coil structure from amino acid 320 to 1310. A 120-kDa kinectin has been observed consistently, and N-terminal sequencing showed that 232 amino acids were missing from the N terminus of full-length kinectin. 120-kDa kinectin was distributed in the supernatant and a low density fraction of vesicles, whereas both forms were in the high density fraction of vesicles. In the electron microscope, the 120-kDa form appeared as a linear molecule of 133 nm in length. In hydrodynamic studies, the cytosolic 120-kDa kinectin was a dimer. Monoclonal antibody molecules (anti-kinectin KR160.9) bound asymmetrically to kinectin often with two antibodies/kinectin, indicative of a parallel coiled-coil. Metabolic labeling with [3H]myristic acid showed that both the 120- and 160-kDa kinectin are myristoylated in chick embryo fibroblasts. The myristoylation of 120-kDa kinectin may provide a mechanism for linking it to a low density fraction of vesicles. Immunoprecipitation with a 160-kDa kinectin-specific antibody brought down the 120-kDa kinectin. Thus, we suggest that kinectin is an extended parallel coiled-coil dimer, often a heterodimer.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/KTN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31738-43
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:9822636-Amino Acid Sequence,
pubmed-meshheading:9822636-Animals,
pubmed-meshheading:9822636-Antibodies, Monoclonal,
pubmed-meshheading:9822636-Binding Sites, Antibody,
pubmed-meshheading:9822636-Cells, Cultured,
pubmed-meshheading:9822636-Chick Embryo,
pubmed-meshheading:9822636-Chickens,
pubmed-meshheading:9822636-DNA, Complementary,
pubmed-meshheading:9822636-Membrane Proteins,
pubmed-meshheading:9822636-Microscopy, Electron,
pubmed-meshheading:9822636-Molecular Sequence Data,
pubmed-meshheading:9822636-Molecular Weight,
pubmed-meshheading:9822636-Myristic Acid,
pubmed-meshheading:9822636-Protein Conformation,
pubmed-meshheading:9822636-RNA, Messenger,
pubmed-meshheading:9822636-Receptors, Cell Surface
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pubmed:year |
1998
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pubmed:articleTitle |
Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin.
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pubmed:affiliation |
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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