Linked Life Data

12105222

Source:http://linkedlifedata.com/resource/pubmed/id/12105222

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
2002-8-30
pubmed:abstractText
Dynamin and its related proteins are a group of mechanochemical proteins involved in the modulation of lipid membranes in various biological processes. Here we investigate the nature of membrane binding of the Arabidopsis dynamin-like 6 (ADL6) involved in vesicle trafficking from the trans-Golgi network to the central vacuole. Fractionation experiments by continuous sucrose gradients and gel filtration revealed that the majority of ADL6 is associated with membranes in vivo. Amino acid sequence analysis revealed that ADL6 has a putative pleckstrin homology (PH) domain. In vitro lipid binding assays demonstrated that ADL6 showed high affinity binding to phosphatidylinositol 3-phosphate (PtdIns-3-P) and that the PH domain was responsible for this interaction. However, the PH domain alone binds equally well to both PtdIns-3-P and phosphatidylinositol 4-phosphate (PtdIns-4-P). Interestingly, the high affinity binding of the PH domain to PtdIns-3-P was restored by a protein-protein interaction between the PH domain and the C-terminal region. In addition, deletion of the inserted regions within the PH domain results in high affinity binding of the PH domain to PtdIns-3-P. These results suggest that ADL6 binds specifically to PtdIns-3-P and that the lipid binding specificity is determined by the interaction between the PH domain and the C-terminal domain of ADL6.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31842-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12105222-Amino Acid Sequence, pubmed-meshheading:12105222-Arabidopsis, pubmed-meshheading:12105222-Arabidopsis Proteins, pubmed-meshheading:12105222-Base Sequence, pubmed-meshheading:12105222-Binding Sites, pubmed-meshheading:12105222-DNA Primers, pubmed-meshheading:12105222-Dynamins, pubmed-meshheading:12105222-GTP Phosphohydrolases, pubmed-meshheading:12105222-Glutathione Transferase, pubmed-meshheading:12105222-Inositol Phosphates, pubmed-meshheading:12105222-Lipid Metabolism, pubmed-meshheading:12105222-Molecular Sequence Data, pubmed-meshheading:12105222-Plant Proteins, pubmed-meshheading:12105222-Polymerase Chain Reaction, pubmed-meshheading:12105222-Recombinant Fusion Proteins, pubmed-meshheading:12105222-Sequence Alignment, pubmed-meshheading:12105222-Sequence Homology, Amino Acid, pubmed-meshheading:12105222-Substrate Specificity
pubmed:year
2002
pubmed:articleTitle
The intermolecular interaction between the PH domain and the C-terminal domain of Arabidopsis dynamin-like 6 determines lipid binding specificity.
pubmed:affiliation
Center for Plant Intracellular Trafficking and the Division of Molecular and Life Sciences, Pohang University of Science and Technology, 790-784, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't