Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6639
pubmed:dateCreated
1997-8-7
pubmed:abstractText
How are signalling molecules organized into different pathways within the same cell? In Drosophila, the inaD gene encodes a protein consisting of five PDZ domains which serves as a scaffold to assemble different components of the phototransduction cascade, including the principal light-activated ion channels, the effector phospholipase C-beta and protein kinase C. Null inaD mutants have a dramatically reorganized subcellular distribution of signalling molecules, and a total loss of transduction complexes. Also, mutants defective in a single PDZ domain produce signalling complexes that lack the target protein and display corresponding defects in their physiology. A picture emerges of a highly organized unit of signalling, a 'transduclisome', with PDZ domains functioning as key elements in the organization of transduction complexes in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
388
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
243-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9230432-Amino Acid Sequence, pubmed-meshheading:9230432-Animals, pubmed-meshheading:9230432-Binding Sites, pubmed-meshheading:9230432-Calcium Channels, pubmed-meshheading:9230432-Drosophila, pubmed-meshheading:9230432-Drosophila Proteins, pubmed-meshheading:9230432-Electrophysiology, pubmed-meshheading:9230432-Eye Proteins, pubmed-meshheading:9230432-Female, pubmed-meshheading:9230432-GTP-Binding Proteins, pubmed-meshheading:9230432-Insect Proteins, pubmed-meshheading:9230432-Male, pubmed-meshheading:9230432-Molecular Sequence Data, pubmed-meshheading:9230432-Mutation, pubmed-meshheading:9230432-Photoreceptor Cells, Invertebrate, pubmed-meshheading:9230432-Protein Kinase C, pubmed-meshheading:9230432-Sequence Homology, Amino Acid, pubmed-meshheading:9230432-Signal Transduction, pubmed-meshheading:9230432-Transient Receptor Potential Channels, pubmed-meshheading:9230432-Type C Phospholipases, pubmed-meshheading:9230432-Vision, Ocular
pubmed:year
1997
pubmed:articleTitle
A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade.
pubmed:affiliation
Howard Hughes Medical Institute, and Department of Biology, University of California at San Diego, La Jolla 92093-0649, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't