Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-5-12
pubmed:abstractText
Apicomplexan parasites exhibit a unique form of substrate-dependent motility, gliding motility, which is essential during their invasion of host cells and during their spread between host cells. This process is dependent on actin filaments and myosin that are both located between the plasma membrane and two underlying membranes of the inner membrane complex. We have identified a protein complex in the apicomplexan parasite Toxoplasma gondii that contains the class XIV myosin required for gliding motility, TgMyoA, its associated light chain, TgMLC1, and two novel proteins, TgGAP45 and TgGAP50. We have localized this complex to the inner membrane complex of Toxoplasma, where it is anchored in the membrane by TgGAP50, an integral membrane glycoprotein. Assembly of the protein complex is spatially controlled and occurs in two stages. These results provide the first molecular description of an integral membrane protein as a specific receptor for a myosin motor, and further our understanding of the motile apparatus underlying gliding motility in apicomplexan parasites.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-105074, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-10564254, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-10579715, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-10749937, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-10854785, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-11062342, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-11420112, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-11713335, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-11854415, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-11887186, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-11980712, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12006666, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12117945, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12139608, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12177058, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12399593, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12456714, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12519984, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12589042, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12642614, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-12718875, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-1607386, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-3585817, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-8008022, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-8022785, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-8235614, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-8601316, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-9010782, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-9383198, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-9566522, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-9625746, http://linkedlifedata.com/resource/pubmed/commentcorrection/15123738-9794629
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9525
pubmed:author
pubmed:copyrightInfo
Copyright the Rockefeller University Press
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
165
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
383-93
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15123738-Amino Acid Sequence, pubmed-meshheading:15123738-Animals, pubmed-meshheading:15123738-Base Sequence, pubmed-meshheading:15123738-Cell Membrane, pubmed-meshheading:15123738-Cell Movement, pubmed-meshheading:15123738-DNA, Complementary, pubmed-meshheading:15123738-Macromolecular Substances, pubmed-meshheading:15123738-Membrane Glycoproteins, pubmed-meshheading:15123738-Molecular Motor Proteins, pubmed-meshheading:15123738-Molecular Sequence Data, pubmed-meshheading:15123738-Myosin Light Chains, pubmed-meshheading:15123738-Myosins, pubmed-meshheading:15123738-Protein Isoforms, pubmed-meshheading:15123738-Protozoan Proteins, pubmed-meshheading:15123738-Receptors, Cell Surface, pubmed-meshheading:15123738-Sequence Homology, Amino Acid, pubmed-meshheading:15123738-Toxoplasma
pubmed:year
2004
pubmed:articleTitle
Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii.
pubmed:affiliation
Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, 108 Taylor Hall, CB# 7090, 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