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Science 3 January 1997:
Vol. 275. no. 5296, pp. 73 - 77
DOI: 10.1126/science.275.5296.73
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Reports

Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains

Z. Songyang, * A. S. Fanning, C. Fu, J. Xu, S. M. Marfatia, A. H. Chishti, A. Crompton, A. C. Chan, J. M. Anderson, L. C. Cantley

The oriented peptide library technique was used to investigate the peptide-binding specificities of nine PDZ domains. Each PDZ domain selected peptides with hydrophobic residues at the carboxyl terminus. Individual PDZ domains selected unique optimal motifs defined primarily by the carboxyl terminal three to seven residues of the peptides. One family of PDZ domains, including those of the Discs Large protein, selected peptides with the consensus motif Glu-(Ser/Thr)-Xxx-(Val/Ile) (where Xxx represents any amino acid) at the carboxyl terminus. In contrast, another family of PDZ domains, including those of LIN-2, p55, and Tiam-1, selected peptides with hydrophobic or aromatic side chains at the carboxyl terminal three residues. On the basis of crystal structures of the PSD-95-3 PDZ domain, the specificities observed with the peptide library can be rationalized.

Z. Songyang, J. Xu, L. C. Cantley, Division of Signal Transduction, Beth Israel Hospital, and Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
A. S. Fanning and J. M. Anderson, Departments of Internal Medicine and Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA.
C. Fu and A. C. Chan, Howard Hughes Medical Institute, Center for Immunology, Department of Medicine and Pathology, Washington University School of Medicine, St. Louis, MO 63110, USA.
S. M. Marfatia and A. H. Chishti, Laboratory of Tumor Cell Biology, Department of Biomedical Research, St. Elizabeth's Medical Center, Tufts University, Boston, MA 02135, USA.
A. Crompton, ONYX Pharmaceuticals, 3031 Research Drive, Building A, Richmond, CA 94806, USA.
*   To whom correspondence should be addressed. Present address: 68-380, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

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The neuronal scaffold protein Shank3 mediates signaling and biological function of the receptor tyrosine kinase Ret in epithelial cells.
G. Schuetz, M. Rosario, J. Grimm, T. M. Boeckers, E. D. Gundelfinger, and W. Birchmeier (2004)
J. Cell Biol. 167, 945-952
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Regulation of Ion Transport by the NHERF Family of PDZ Proteins.
S. Shenolikar, J. W. Voltz, R. Cunningham, and E. J. Weinman (2004)
Physiology 19, 362-369
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Delta proteins and MAGI proteins: an interaction of Notch ligands with intracellular scaffolding molecules and its significance for zebrafish development.
G. J. Wright, J. D. Leslie, L. Ariza-McNaughton, and J. Lewis (2004)
Development 131, 5659-5669
   Abstract »    Full Text »    PDF »
ATP-binding Cassette Transporter A1 Contains a Novel C-terminal VFVNFA Motif That Is Required for Its Cholesterol Efflux and ApoA-I Binding Activities.
M. L. Fitzgerald, K.-i. Okuhira, G. F. Short III, J. J. Manning, S. A. Bell, and M. W. Freeman (2004)
J. Biol. Chem. 279, 48477-48485
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PSD-95 and Lin-7b Interact with Acid-sensing Ion Channel-3 and Have Opposite Effects on H+-gated Current.
A. M. Hruska-Hageman, C. J. Benson, A. S. Leonard, M. P. Price, and M. J. Welsh (2004)
J. Biol. Chem. 279, 46962-46968
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The C-terminal Tail of Presenilin Regulates Omi/HtrA2 Protease Activity.
S. Gupta, R. Singh, P. Datta, Z. Zhang, C. Orr, Z. Lu, G. DuBois, A. S. Zervos, M. H. Meisler, S. M. Srinivasula, et al. (2004)
J. Biol. Chem. 279, 45844-45854
   Abstract »    Full Text »    PDF »
The Multivalent PDZ Domain-containing Protein PDZK1 Regulates Transport Activity of Renal Urate-Anion Exchanger URAT1 via Its C Terminus.
N. Anzai, H. Miyazaki, R. Noshiro, S. Khamdang, A. Chairoungdua, H.-J. Shin, A. Enomoto, S. Sakamoto, T. Hirata, K. Tomita, et al. (2004)
J. Biol. Chem. 279, 45942-45950
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The PDZ Domain of the SpoIVB Transmembrane Signaling Protein Enables cis-trans Interactions Involving Multiple Partners Leading to the Activation of the Pro-{sigma}K Processing Complex in Bacillus subtilis.
T. C. Dong and S. M. Cutting (2004)
J. Biol. Chem. 279, 43468-43478
   Abstract »    Full Text »    PDF »
From The Cover: The immunoglobulin family member dendrite arborization and synapse maturation 1 (Dasm1) controls excitatory synapse maturation.
S.-H. Shi, T. Cheng, L. Y. Jan, and Y.-N. Jan (2004)
PNAS 101, 13346-13351
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Autocatalytic Processing of HtrA2/Omi Is Essential for Induction of Caspase-dependent Cell Death through Antagonizing XIAP.
Y.-M. Seong, J.-Y. Choi, H.-J. Park, K.-J. Kim, S.-G. Ahn, G.-H. Seong, I.-K. Kim, S. Kang, and H. Rhim (2004)
J. Biol. Chem. 279, 37588-37596
   Abstract »    Full Text »    PDF »
Connexin43 Interacts with NOV: A POSSIBLE MECHANISM FOR NEGATIVE REGULATION OF CELL GROWTH IN CHORIOCARCINOMA CELLS.
A. Gellhaus, X. Dong, S. Propson, K. Maass, L. Klein-Hitpass, M. Kibschull, O. Traub, K. Willecke, B. Perbal, S. J. Lye, et al. (2004)
J. Biol. Chem. 279, 36931-36942
   Abstract »    Full Text »    PDF »
NEURONAL PDZ DOMAINS: A Promising New Molecular Target for Inhaled Anesthetics?.
Y.-X. Tao and R. A. Johns (2004)
Mol. Interv. 4, 215-221
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A dileucine motif targets the sulfate anion transporter sat-1 to the basolateral membrane in renal cell lines.
R. R. Regeer and D. Markovich (2004)
Am J Physiol Cell Physiol 287, C365-C372
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Discs large (Dlg1) complexes in lymphocyte activation.
R. Xavier, S. Rabizadeh, K. Ishiguro, N. Andre, J. B. Ortiz, H. Wachtel, D. G. Morris, M. Lopez-Ilasaca, A. C. Shaw, W. Swat, et al. (2004)
J. Cell Biol. 166, 173-178
   Abstract »    Full Text »    PDF »
Endothelial Cell-to-Cell Junctions: Molecular Organization and Role in Vascular Homeostasis.
G. Bazzoni and E. Dejana (2004)
Physiol Rev 84, 869-901
   Abstract »    Full Text »    PDF »
Signaling at the Slit Diaphragm.
T. Benzing (2004)
J. Am. Soc. Nephrol. 15, 1382-1391
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A Novel PTB-PDZ Domain Interaction Mediates Isoform-specific Ubiquitylation of Mammalian Numb.
J. Nie, S. S.-C. Li, and C. J. McGlade (2004)
J. Biol. Chem. 279, 20807-20815
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Gap junctions and connexin-interacting proteins.
B. N.G Giepmans (2004)
Cardiovasc Res 62, 233-245
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A Multiprotein Trafficking Complex Composed of SAP97, CASK, Veli, and Mint1 Is Associated with Inward Rectifier Kir2 Potassium Channels.
D. Leonoudakis, L. R. Conti, C. M. Radeke, L. M. M. McGuire, and C. A. Vandenberg (2004)
J. Biol. Chem. 279, 19051-19063
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Carboxy Terminus of Glucose Transporter 3 Contains an Apical Membrane Targeting Domain.
K. Inukai, A. M. Shewan, W. S. Pascoe, S. Katayama, D. E. James, and Y. Oka (2004)
Mol. Endocrinol. 18, 339-349
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CLMP, a Novel Member of the CTX Family and a New Component of Epithelial Tight Junctions.
E. Raschperger, U. Engstrom, R. F. Pettersson, and J. Fuxe (2004)
J. Biol. Chem. 279, 796-804
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Junctional adhesion molecules (JAMs): more molecules with dual functions?.
K. Ebnet, A. Suzuki, S. Ohno, and D. Vestweber (2004)
J. Cell Sci. 117, 19-29
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