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p300 interacts with the nuclear proto-oncoprotein SYT as part of the active control of cell adhesion.

作者信息

Eid J E, Kung A L, Scully R, Livingston D M

机构信息

Dana-Farber Cancer Institute and Harvard Medical School, Boston, Massachusetts 02115, USA.

出版信息

Cell. 2000 Sep 15;102(6):839-48. doi: 10.1016/s0092-8674(00)00072-6.

Abstract

Complexes containing p300, but not CBP, and the nuclear proto-oncoprotein SYT were detected in confluent cultures of G1-arrested cells but not in sparse cells or during S or G2. SYT sequences constitute the N-terminal segment of a fusion oncogene product, SYT-SSX, routinely detected in synovial sarcoma, an aggressive human tumor. SYT/p300 complex formation promotes cell adhesion to a fibronectin matrix, as reflected by compromise of this process in cells expressing SYT dl mutants that retain p300 binding activity and in the primary fibroblasts of p300 but not CBP heterozygous null mice. The mechanism linking the action of SYT/p300 complexes to adhesion function is, at least in part, transcription activation-independent and results in proper activation of beta1 integrin, a major adhesion receptor.

摘要

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