PMID- 10037602
OWN - NLM
STAT- MEDLINE
DCOM- 19990312
LR  - 20190619
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 283
IP  - 5406
DP  - 1999 Feb 26
TI  - Function of WW domains as phosphoserine- or phosphothreonine-binding modules.
PG  - 1325-8
AB  - 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.
FAU - Lu, P J
AU  - Lu PJ
AD  - Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, 
      Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA
      02215, USA.
FAU - Zhou, X Z
AU  - Zhou XZ
FAU - Shen, M
AU  - Shen M
FAU - Lu, K P
AU  - Lu KP
LA  - eng
GR  - R01GM56230/GM/NIGMS NIH HHS/United States
GR  - R01GM58556/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Endosomal Sorting Complexes Required for Transport)
RN  - 0 (NIMA-Interacting Peptidylprolyl Isomerase)
RN  - 0 (Phosphopeptides)
RN  - 0 (Phosphoproteins)
RN  - 1114-81-4 (Phosphothreonine)
RN  - 17885-08-4 (Phosphoserine)
RN  - EC 2.3.2.26 (Nedd4 Ubiquitin Protein Ligases)
RN  - EC 2.3.2.26 (Nedd4 protein, human)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 3.1.3.48 (CDC25C protein, human)
RN  - EC 3.1.3.48 (cdc25 Phosphatases)
RN  - EC 5.2.1.8 (PIN1 protein, human)
RN  - EC 5.2.1.8 (Peptidylprolyl Isomerase)
RN  - EC 6.- (Ligases)
SB  - IM
CIN - Science. 1999 Feb 26;283(5406):1247, 1249. PMID: 10084927
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Calcium-Binding Proteins/chemistry/*metabolism
MH  - Cell Cycle Proteins/metabolism
MH  - Endosomal Sorting Complexes Required for Transport
MH  - HeLa Cells
MH  - Humans
MH  - *Ligases
MH  - NIMA-Interacting Peptidylprolyl Isomerase
MH  - Nedd4 Ubiquitin Protein Ligases
MH  - Peptidylprolyl Isomerase/chemistry/genetics/*metabolism
MH  - Phosphopeptides/metabolism
MH  - Phosphoproteins/*metabolism
MH  - Phosphorylation
MH  - Phosphoserine/*metabolism
MH  - Phosphothreonine/*metabolism
MH  - Point Mutation
MH  - Signal Transduction
MH  - *Ubiquitin-Protein Ligases
MH  - *cdc25 Phosphatases
EDAT- 1999/02/26 00:00
MHDA- 1999/02/26 00:01
CRDT- 1999/02/26 00:00
PHST- 1999/02/26 00:00 [pubmed]
PHST- 1999/02/26 00:01 [medline]
PHST- 1999/02/26 00:00 [entrez]
AID - 10.1126/science.283.5406.1325 [doi]
PST - ppublish
SO  - Science. 1999 Feb 26;283(5406):1325-8. doi: 10.1126/science.283.5406.1325.