Identification of a Ten-Amino Acid Proline-Rich SH3 Binding Site

American Association for the Advancement of Science (AAAS) - Tập 259 Số 5098 - Trang 1157-1161 - 1993
Ruibao Ren1, Bruce J. Mayer1, Piera Cicchetti1, David Baltimore1
1Rockefeller University, New York, NY 10021

Tóm tắt

The Src homology 3 (SH3) region is a small protein domain present in a very large group of proteins, including cytoskeletal elements and signaling proteins. It is believed that SH3 domains serve as modules that mediate protein-protein associations and, along with Src homology 2 (SH2) domains, regulate cytoplasmic signaling. The SH3 binding sites of two SH3 binding proteins were localized to a nine- or ten-amino acid stretch very rich in proline residues. Similar SH3 binding motifs exist in the formins, proteins that function in pattern formation in embryonic limbs of the mouse, and one subtype of the muscarinic acetylcholine receptor. Identification of the SH3 binding site provides a basis for understanding the interaction between the SH3 domains and their targets.

Từ khóa


Tài liệu tham khảo

TRENDS IN PHARMACOLOGICAL SCIENCES Supplement vii (1989).

ALEXANDROPOULOS K unpublished data.

Ausubel F. M. Current Protocols in Molecular Biology (1987).

BENNERIAH, Y, ALTERNATIVE 5' EXONS IN C-ABL MESSENGER-RNA, CELL 44: 577 (1986).

10.1126/science.3037705

10.1126/science.1379745

CLARK, S.G., C-ELEGANS CELL-SIGNALING GENE SEM-5 ENCODES A PROTEIN WITH SH2 AND SH3 DOMAINS, NATURE 356: 340 (1992).

DICKIE, M.M., MOUSE NEWS LETTER 38: 24 (1968).

FRANZ, W.M., DELETION OF AN N-TERMINAL REGULATORY DOMAIN OF THE C-ABL TYROSINE KINASE ACTIVATES ITS ONCOGENIC POTENTIAL, EMBO JOURNAL 8: 137 (1989).

GREEN, M.C., MOUSE NEWS LETTER 31: 27 (1964).

Grueneberg H. The Pathology of Development. A Study of Inherited Skeletal Disorders in Animals (1963).

HIRAI, H, SITE-DIRECTED MUTAGENESIS OF THE SH2-CODING AND SH3-CODING DOMAINS OF C-SRC PRODUCES VARIED PHENOTYPES, INCLUDING ONCOGENIC ACTIVATION OF P60C-SRC, MOLECULAR AND CELLULAR BIOLOGY 10: 1307 (1990).

JACKSON, P, EMBO JOURNAL 8: 449 (1989).

JENKINS N unpublished data.

KATO, J.Y., AMINO-ACID SUBSTITUTIONS SUFFICIENT TO CONVERT THE NONTRANSFORMING P60C-SRC PROTEIN TO A TRANSFORMING PROTEIN, MOLECULAR AND CELLULAR BIOLOGY 6: 4155 (1986).

10.1126/science.1708916

LEHMANN, J.M., NCK, A MELANOMA CDNA-ENCODING A CYTOPLASMIC PROTEIN CONSISTING OF THE SRC HOMOLOGY UNITS SH2 AND SH3, NUCLEIC ACIDS RESEARCH 18: 1048 (1990).

10.1016/0092-8674(92)90167-B

10.1126/science.1553544

MASS, R.L., NATURE 346: 853 (1990).

MAYER, B.J., THE NONCATALYTIC SRC HOMOLOGY REGION-2 SEGMENT OF ABL TYROSINE KINASE BINDS TO TYROSINE-PHOSPHORYLATED CELLULAR PROTEINS WITH HIGH-AFFINITY, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 88: 627 (1991).

MUSACCHIO, A, SH3 - AN ABUNDANT PROTEIN DOMAIN IN SEARCH OF A FUNCTION, FEBS LETTERS 307: 55 (1992).

10.1038/359851a0

NATHANSON, N.M., MOLECULAR-PROPERTIES OF THE MUSCARINIC ACETYLCHOLINE-RECEPTOR, ANNUAL REVIEW OF NEUROSCIENCE 10: 195 (1987).

PAWSON, T, CURR OPIN STRUC BIOL 2: 432 (1992).

PAWSON, T, CELL SIGNALING - CONVICTION BY GENETICS, NATURE 356: 285 (1992).

PERALTA, E.G., DISTINCT PRIMARY STRUCTURES, LIGAND-BINDING PROPERTIES AND TISSUE-SPECIFIC EXPRESSION OF 4 HUMAN MUSCARINIC ACETYLCHOLINE-RECEPTORS, EMBO JOURNAL 6: 3923 (1987).

POTTS, W.M., ONCOGENE RES 3: 343 (1988).

REN R unpublished data.

Richardson J. S. Prediction of Protein Structure and the Principles of Protein Conformation (1989).

SEIDELDUGAN, C, EFFECTS OF SH2 AND SH3 DELETIONS ON THE FUNCTIONAL ACTIVITIES OF WILD-TYPE AND TRANSFORMING VARIANTS OF C-SRC, MOLECULAR AND CELLULAR BIOLOGY 12: 1835 (1992).

Stryer L. Biochemistry (1988).

SWEET, H.O., MOUSE NEWS LETTER 66: 66 (1982).

WOYCHIK, R.P., AN INHERITED LIMB DEFORMITY CREATED BY INSERTIONAL MUTAGENESIS IN A TRANSGENIC MOUSE, NATURE 318: 36 (1985).

WOYCHIK, R.P., FORMINS - PROTEINS DEDUCED FROM THE ALTERNATIVE TRANSCRIPTS OF THE LIMB DEFORMITY GENE, NATURE 346: 850 (1990).

YATANI, A, RAS P21 AND GAP INHIBIT COUPLING OF MUSCARINIC RECEPTORS TO ATRIAL K+ CHANNELS, CELL 61: 769 (1990).

10.1126/science.1280858