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Science 26 February 1999:
Vol. 283. no. 5406, pp. 1325 - 1328
DOI: 10.1126/science.283.5406.1325
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Reports

Function of WW Domains as Phosphoserine- or Phosphothreonine-Binding Modules

Pei-Jung Lu, * Xiao Zhen Zhou, * Minhui Shen, Kun Ping Lu dagger

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.

Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: klu{at}caregroup.harvard.edu

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J. Biol. Chem. 274, 26485-26492
   Abstract »    Full Text »    PDF »
Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain.
J. Li, G. P. Smith, and J. C. Walker (1999)
PNAS 96, 7821-7826
   Abstract »    Full Text »    PDF »
A Single Point Mutation in a Group I WW Domain Shifts Its Specificity to That of Group II WW Domains.
X. Espanel and M. Sudol (1999)
J. Biol. Chem. 274, 17284-17289
   Abstract »    Full Text »    PDF »
Phosphatase 2A and polo kinase, two antagonistic regulators of cdc25 activation and MPF auto-amplification.
A Karaiskou, C Jessus, T Brassac, and R Ozon (1999)
J. Cell Sci. 112, 3747-3756
   Abstract »    PDF »
The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts with Cdc2 complexes and is required for inhibition of G(2)/M progression.
N. Wells, N Watanabe, T Tokusumi, W Jiang, M. Verdecia, and T Hunter (1999)
J. Cell Sci. 112, 3361-3371
   Abstract »    PDF »
Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity and Pin1 Function.
P.-J. Lu, X. Z. Zhou, Y.-C. Liou, J. P. Noel, and K. P. Lu (2002)
J. Biol. Chem. 277, 2381-2384
   Abstract »    Full Text »    PDF »
Casein Kinase I-dependent Phosphorylation within a PEST Sequence and Ubiquitination at Nearby Lysines Signal Endocytosis of Yeast Uracil Permease.
C. Marchal, R. Haguenauer-Tsapis, and D. Urban-Grimal (2000)
J. Biol. Chem. 275, 23608-23614
   Abstract »    Full Text »    PDF »
Rsp5 WW Domains Interact Directly with the Carboxyl-terminal Domain of RNA Polymerase II.
A. Chang, S. Cheang, X. Espanel, and M. Sudol (2000)
J. Biol. Chem. 275, 20562-20571
   Abstract »    Full Text »    PDF »
Identification of an Essential Amino Acid Motif within the C Terminus of the Pituitary Adenylate Cyclase-activating Polypeptide Type I Receptor That Is Critical for Signal Transduction but Not for Receptor Internalization.
R.-M. Lyu, P. M. Germano, J. K. Choi, S. V. Le, and J. R. Pisegna (2000)
J. Biol. Chem. 275, 36134-36142
   Abstract »    Full Text »    PDF »
p13SUC1 and the WW Domain of PIN1 Bind to the Same Phosphothreonine-Proline Epitope.
I. Landrieu, B. Odaert, J.-M. Wieruszeski, H. Drobecq, P. Rousselot-Pailley, D. Inze, and G. Lippens (2001)
J. Biol. Chem. 276, 1434-1438
   Abstract »    Full Text »    PDF »
Functional Replacement of the Essential ESS1 in Yeast by the Plant Parvulin DlPar13.
M. Metzner, G. Stoller, K. P. Rucknagel, K. P. Lu, G. Fischer, M. Luckner, and G. Kullertz (2001)
J. Biol. Chem. 276, 13524-13529
   Abstract »    Full Text »    PDF »
Functional Conservation of Phosphorylation-specific Prolyl Isomerases in Plants.
J.-L. Yao, O. Kops, P.-J. Lu, and K. P. Lu (2001)
J. Biol. Chem. 276, 13517-13523
   Abstract »    Full Text »    PDF »
Recognition and Ubiquitination of Notch by Itch, a Hect-type E3 Ubiquitin Ligase.
L. Qiu, C. Joazeiro, N. Fang, H.-Y. Wang, C. Elly, Y. Altman, D. Fang, T. Hunter, and Y.-C. Liu (2000)
J. Biol. Chem. 275, 35734-35737
   Abstract »    Full Text »    PDF »
Signal Transduction by the CEACAM1 Tumor Suppressor. PHOSPHORYLATION OF SERINE 503 IS REQUIRED FOR GROWTH-INHIBITORY ACTIVITY.
V. T. Estrera, D.-T. Chen, W. Luo, D. C. Hixson, and S.-H. Lin (2001)
J. Biol. Chem. 276, 15547-15553
   Abstract »    Full Text »    PDF »
Yes-associated Protein and p53-binding Protein-2 Interact through Their WW and SH3 Domains.
X. Espanel and M. Sudol (2001)
J. Biol. Chem. 276, 14514-14523
   Abstract »    Full Text »    PDF »
1H NMR Study on the Binding of Pin1 Trp-Trp Domain with Phosphothreonine Peptides.
R. Wintjens, J.-M. Wieruszeski, H. Drobecq, P. Rousselot-Pailley, L. Buee, G. Lippens, and I. Landrieu (2001)
J. Biol. Chem. 276, 25150-25156
   Abstract »    Full Text »    PDF »
Physical Interaction with Yes-associated Protein Enhances p73 Transcriptional Activity.
S. Strano, E. Munarriz, M. Rossi, L. Castagnoli, Y. Shaul, A. Sacchi, M. Oren, M. Sudol, G. Cesareni, and G. Blandino (2001)
J. Biol. Chem. 276, 15164-15173
   Abstract »    Full Text »    PDF »
Telomeric Protein Pin2/TRF1 as an Important ATM Target in Response to Double Strand DNA Breaks.
S. Kishi, X. Z. Zhou, Y. Ziv, C. Khoo, D. E. Hill, Y. Shiloh, and K. P. Lu (2001)
J. Biol. Chem. 276, 29282-29291
   Abstract »    Full Text »    PDF »


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