Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-3-17
pubmed:databankReference
pubmed:abstractText
Dynamin is a GTP-, microtubule-, and phospholipid-binding protein that is expressed primarily in brain. In Drosophila, the shibire gene encodes a homologue of dynamin; mutations in this gene result in a defect in endocytosis, suggesting a function for dynamin in endocytic membrane traffic. In the present study we show that there are at least two distinct dynamin genes in mammals whose products are referred to as dynamins I and II. The two dynamins are similar to each other (79% identity) and are both equally homologous to the Drosophila shibire gene product (66% identity). The highest degree of identity between dynamins is observed in their N-terminal halves, whereas their C termini exhibit little homology. Transcripts of both dynamin genes are subject to at least two alternative splicing events, the first of which is identically found in both dynamins, whereas the second site of alternative splicing is different between the two types of dynamins. The first alternatively spliced sequence of the dynamins consists of an interior region that is present in two distinct but homologous forms in both dynamins, suggesting alternative use of exons in both genes at identical positions. The second site of alternative splicing results in the generation of different C termini in dynamin I and in the inclusion or exclusion of an interior four-amino acid sequence in dynamin II. The two dynamins exhibit remarkable differences in their tissue distribution and regulation. Dynamin I is almost exclusively expressed in the central nervous system. Conversely, dynamin II is expressed ubiquitously in all tissues tested. Previous studies revealed that the GTPase activity of dynamin I is regulated by phosphorylation by protein kinase C in nerve terminals. Expression of dynamins I and II by transfection in COS cells demonstrates that only dynamin I but not dynamin II is a substrate for protein kinase C. Our data suggest a specialization in the endocytic functions and the regulation of dynamins between neural and non-neural tissues in mammals.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4547-54
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:8308025-Amino Acid Sequence, pubmed-meshheading:8308025-Animals, pubmed-meshheading:8308025-Base Sequence, pubmed-meshheading:8308025-Cloning, Molecular, pubmed-meshheading:8308025-DNA Primers, pubmed-meshheading:8308025-Drosophila Proteins, pubmed-meshheading:8308025-Dynamin I, pubmed-meshheading:8308025-Dynamins, pubmed-meshheading:8308025-GTP Phosphohydrolases, pubmed-meshheading:8308025-Genes, pubmed-meshheading:8308025-Genes, Insect, pubmed-meshheading:8308025-Molecular Sequence Data, pubmed-meshheading:8308025-Phosphoproteins, pubmed-meshheading:8308025-Phosphorylation, pubmed-meshheading:8308025-Protein Kinase C, pubmed-meshheading:8308025-Rats, pubmed-meshheading:8308025-Sequence Alignment, pubmed-meshheading:8308025-Sequence Homology, Amino Acid, pubmed-meshheading:8308025-Sequence Homology, Nucleic Acid, pubmed-meshheading:8308025-Tissue Distribution
pubmed:year
1994
pubmed:articleTitle
Differential expression and regulation of multiple dynamins.
pubmed:affiliation
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't