Linked Life Data

9169476

Source:http://linkedlifedata.com/resource/pubmed/id/9169476

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1997-6-26
pubmed:abstractText
We have recently demonstrated that the nonvisual arrestins, beta-arrestin and arrestin3, interact with high affinity and stoichiometrically with clathrin, and we postulated that this interaction mediates internalization of G protein-coupled receptors (Goodman, O. B., Jr., Krupnick, J. G., Santini, F., Gurevich, V. V., Penn, R. B., Gagnon, A. W., Keen, J. H., and Benovic, J. L. (1996) Nature 383, 447-450). In this study, we localized the clathrin binding domain of arrestin3 using a variety of approaches. Truncation mutagenesis demonstrated that the COOH-terminal half of arrestin3 is required for clathrin interaction. Assessment of the clathrin binding properties of various glutathione S-transferase-arrestin3 fusion proteins indicated that the predominant clathrin binding domain is contained within residues 367-385. Alanine scanning mutagenesis further localized this domain to residues 371-379, and site-directed mutagenesis demonstrated the critical importance of both hydrophobic (Leu-373, Ile-374, and Phe-376) and acidic (Glu-375 and Glu-377) residues in the arrestin3/clathrin interaction. These results are complementary to the observation that hydrophobic and basic residues in clathrin are critical for its interaction with nonvisual arrestins (Goodman, O. B. , Jr., Krupnick, J. G., Gurevich, V. V., Benovic, J. L., and Keen, J. H. (1997) J. Biol. Chem. 272, 15017-15022). Lastly, an arrestin3 mutant in which Leu-373, Ile-374, and Phe-376 were mutated to Ala was significantly defective in its ability to promote beta2-adrenergic receptor internalization in COS-1 cells when compared with wild-type arrestin3. Taken together, these results implicate a discrete region of arrestin3 in high affinity binding to clathrin, an interaction critical for agonist-promoted internalization of the beta2-adrenergic receptor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15011-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9169476-Alanine, pubmed-meshheading:9169476-Amino Acid Sequence, pubmed-meshheading:9169476-Animals, pubmed-meshheading:9169476-Arrestins, pubmed-meshheading:9169476-Binding Sites, pubmed-meshheading:9169476-COS Cells, pubmed-meshheading:9169476-Cattle, pubmed-meshheading:9169476-Clathrin, pubmed-meshheading:9169476-Glutathione Transferase, pubmed-meshheading:9169476-Kinetics, pubmed-meshheading:9169476-Molecular Sequence Data, pubmed-meshheading:9169476-Mutagenesis, Site-Directed, pubmed-meshheading:9169476-Protein Biosynthesis, pubmed-meshheading:9169476-Receptors, Adrenergic, beta-2, pubmed-meshheading:9169476-Recombinant Fusion Proteins, pubmed-meshheading:9169476-Sequence Deletion, pubmed-meshheading:9169476-Transcription, Genetic, pubmed-meshheading:9169476-Transfection
pubmed:year
1997
pubmed:articleTitle
Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus.
pubmed:affiliation
Department of Biochemistry, Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't