Linked Life Data

11870218

Source:http://linkedlifedata.com/resource/pubmed/id/11870218

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 5
pubmed:dateCreated
2002-2-28
pubmed:abstractText
Class V myosins are one of the most ancient and widely distributed groups of the myosin superfamily and are hypothesized to function as motors for actin-dependent organelle transport. We report the discovery and initial characterization of a novel member of this family, human myosin-Vc (Myo5c). The Myo5c protein sequence shares approximately 50% overall identity with the two other class V myosins in vertebrates, myosin-Va (Myo5a) and myosin-Vb (Myo5b). Systematic analysis of the mRNA and protein distribution of these myosins indicates that Myo5a is most abundant in brain, whereas Myo5b and Myo5c are expressed chiefly in non-neuronal tissues. Myo5c is particularly abundant in epithelial and glandular tissues including pancreas, prostate, mammary, stomach, colon and lung. Immunolocalization in colon and exocrine pancreas indicates that Myo5c is expressed chiefly in epithelial cells. A dominant negative approach using a GFP-Myo5c tail construct in HeLa cells reveals that the Myo5c tail selectively colocalizes with and perturbs a membrane compartment containing the transferrin receptor and rab8. Transferrin also accumulates in this compartment, suggesting that Myo5c is involved in transferrin trafficking. As a class V myosin of epithelial cells, Myo5c is likely to power actin-based membrane trafficking in many physiologically crucial tissues of the human body.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
991-1004
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11870218-Amino Acid Sequence, pubmed-meshheading:11870218-Animals, pubmed-meshheading:11870218-Base Sequence, pubmed-meshheading:11870218-Cell Compartmentation, pubmed-meshheading:11870218-Cloning, Molecular, pubmed-meshheading:11870218-Colon, pubmed-meshheading:11870218-Epithelial Cells, pubmed-meshheading:11870218-Green Fluorescent Proteins, pubmed-meshheading:11870218-HeLa Cells, pubmed-meshheading:11870218-Humans, pubmed-meshheading:11870218-Intracellular Membranes, pubmed-meshheading:11870218-Luminescent Proteins, pubmed-meshheading:11870218-Mice, pubmed-meshheading:11870218-Molecular Sequence Data, pubmed-meshheading:11870218-Myosin Type V, pubmed-meshheading:11870218-Myosins, pubmed-meshheading:11870218-Pancreas, pubmed-meshheading:11870218-Protein Structure, Tertiary, pubmed-meshheading:11870218-Protein Transport, pubmed-meshheading:11870218-Receptors, Transferrin, pubmed-meshheading:11870218-Transferrin, pubmed-meshheading:11870218-Viscera, pubmed-meshheading:11870218-rab GTP-Binding Proteins
pubmed:year
2002
pubmed:articleTitle
Human myosin-Vc is a novel class V myosin expressed in epithelial cells.
pubmed:affiliation
Department of Cell and Molecular Physiology, Medical Science Research Building, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't