Publication Date:
1999-02-26
Description:
Protein-interacting modules help determine the specificity of signal transduction events, and protein phosphorylation can modulate the assembly of such modules into specific signaling complexes. Although phosphotyrosine-binding modules have been well-characterized, phosphoserine- or phosphothreonine-binding modules have not been described. WW domains are small protein modules found in various proteins that participate in cell signaling or regulation. WW domains of the essential mitotic prolyl isomerase Pin1 and the ubiquitin ligase Nedd4 bound to phosphoproteins, including physiological substrates of enzymes, in a phosphorylation-dependent manner. The Pin1 WW domain functioned as a phosphoserine- or phosphothreonine-binding module, with properties similar to those of SRC homology 2 domains. Phosphoserine- or phosphothreonine-binding activity was required for Pin1 to interact with its substrates in vitro and to perform its essential function in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, P J -- Zhou, X Z -- Shen, M -- Lu, K P -- R01GM56230/GM/NIGMS NIH HHS/ -- R01GM58556/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Feb 26;283(5406):1325-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10037602" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Amino Acid Substitution
;
Calcium-Binding Proteins/chemistry/*metabolism
;
Cell Cycle Proteins/metabolism
;
Endosomal Sorting Complexes Required for Transport
;
HeLa Cells
;
Humans
;
*Ligases
;
Peptidylprolyl Isomerase/chemistry/genetics/*metabolism
;
Phosphopeptides/metabolism
;
Phosphoproteins/*metabolism
;
Phosphorylation
;
Phosphoserine/*metabolism
;
Phosphothreonine/*metabolism
;
Point Mutation
;
Signal Transduction
;
*Ubiquitin-Protein Ligases
;
*cdc25 Phosphatases
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
