Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
43
pubmed:dateCreated
1998-11-17
pubmed:abstractText
Cytoplasmic dynein contains a series of accessory proteins associated with the motor containing heavy chains.1 These include three distinct classes of light chains (Mr < approximately 22 000). Here we demonstrate that a previously cloned protein termed rp3 is a bona fide Mr 14 000 light chain component of this microtubule motor complex. The rp3 polypeptide is approximately 55% identical to the Tctex1 dynein light chain, and together, these two proteins define one branch of a diverse family of Mr 14 000 light chains associated with both cytoplasmic and flagellar dyneins. The Tctex1 and rp3 light chains are differentially expressed in various tissues: rp3 is most prevalent in liver and brain cytoplasmic dynein, whereas those tissues contain the least amounts of Tctex1. Immunofluorescence analysis was consistent with the tissue-specific distribution of these proteins and revealed that both rp3 and Tctex1 are present in multiple perinuclear punctate particles. Furthermore, in two cell lines, rp3 was found associated with an elongated structure located in the layer of cytoplasm above the nucleus. Electrophoretic/immunological analysis indicates that there are only single isoforms for these proteins in brain and PC-12 cells, suggesting that alterations in the Mr 14 000 light chains of dynein are achieved at the level of the individual proteins and not by posttranslational modification. Dissection of the cytoplasmic dynein complex revealed that Tctex1, an Mr 8000 LC dimer, and IC74 associate to define a basal-located intermediate chain/light chain complex analogous to that found in flagellar outer arm dynein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15033-41
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9790665-Amino Acid Sequence, pubmed-meshheading:9790665-Animals, pubmed-meshheading:9790665-Brain Chemistry, pubmed-meshheading:9790665-Cell Line, pubmed-meshheading:9790665-Cytoplasm, pubmed-meshheading:9790665-Dyneins, pubmed-meshheading:9790665-Eye Proteins, pubmed-meshheading:9790665-Humans, pubmed-meshheading:9790665-Kidney, pubmed-meshheading:9790665-Mice, pubmed-meshheading:9790665-Microtubule Proteins, pubmed-meshheading:9790665-Microtubule-Associated Proteins, pubmed-meshheading:9790665-Molecular Sequence Data, pubmed-meshheading:9790665-Molecular Weight, pubmed-meshheading:9790665-Multigene Family, pubmed-meshheading:9790665-Nuclear Proteins, pubmed-meshheading:9790665-Organ Specificity, pubmed-meshheading:9790665-PC12 Cells, pubmed-meshheading:9790665-Protein Biosynthesis, pubmed-meshheading:9790665-Proteins, pubmed-meshheading:9790665-Rats, pubmed-meshheading:9790665-t-Complex Genome Region
pubmed:year
1998
pubmed:articleTitle
Cytoplasmic dynein contains a family of differentially expressed light chains.
pubmed:affiliation
Department of Biochemistry, Center for Biomedical Imaging Technology, University of Connecticut Health Center, Farmington 06032-3305, USA. king@panda.uch.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't