Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family.

In this study, a protein that interacts with sequences encoded by the first exon of the protein kinase Bcr was cloned. The Bcr-associated protein 1 (Bap-1) is a member of the 14-3-3 family of proteins. Bap-1 interacts with full-length c-Bcr and with the chimeric Bcr-Abl tyrosine kinase of Philadelphia chromosome (Ph1)-positive human leukemias. Bap-1 is a substrate for the Bcr serine-threonine kinase and is also phosphorylated on tyrosine by Bcr-Abl but not by c-Abl. Bap-1 may function in the regulation of c-Bcr and may contribute to the transforming activity of Bcr-Abl in vivo. 14-3-3 proteins are essential for cell proliferation and have a role in determining the timing of mitosis in yeast. Through direct binding to sequences present in Bcr and in other proteins implicated in signaling, the mammalian 14-3-3 proteins may link specific signaling protein components to mitogenic and cell-cycle control pathways.

[1]  K. Xia,et al.  Interaction of the protein kinase Raf-1 with 14-3-3 proteins. , 1994, Science.

[2]  T. Roberts,et al.  Association of polyomavirus middle tumor antigen with 14-3-3 proteins. , 1994, Science.

[3]  A. Carr,et al.  14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast. , 1994, Science.

[4]  J. Hancock,et al.  Activation of Raf as a result of recruitment to the plasma membrane. , 1994, Science.

[5]  C. Sawyers,et al.  Differential complementation of Bcr-Abl point mutants with c-Myc. , 1994, Science.

[6]  T Pawson,et al.  Bcr‐Abl oncoproteins bind directly to activators of the Ras signalling pathway. , 1994, The EMBO journal.

[7]  Mark S. Boguski,et al.  Proteins regulating Ras and its relatives , 1993, Nature.

[8]  C. Marshall,et al.  rho family GTPase activating proteins p190, bcr and rhoGAP show distinct specificities in vitro and in vivo. , 1993, The EMBO journal.

[9]  J. Wang,et al.  A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins. , 1993, Molecular and cellular biology.

[10]  R. Weinberg,et al.  The pathway to signal achievement , 1993, Nature.

[11]  Nanxin Li,et al.  BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein , 1993, Cell.

[12]  J. Thompson,et al.  The PH domain: a common piece in the structural patchwork of signalling proteins. , 1993, Trends in biochemical sciences.

[13]  R. Collier,et al.  The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[14]  O. Witte,et al.  SH1 domain autophosphorylation of P210 BCR/ABL is required for transformation but not growth factor independence , 1993, Molecular and cellular biology.

[15]  T. M. Roberts.  A signal chain of events , 1992, Nature.

[16]  A. Aitken,et al.  14-3-3 proteins : a highly conserved widespread family of eukaryotic proteins , 2003 .

[17]  C. Sawyers,et al.  Dominant negative MYC blocks transformation by ABL oncogenes , 1992, Cell.

[18]  A. Toker,et al.  Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from sheep brain. Amino acid sequence of phosphorylated forms. , 1992, European journal of biochemistry.

[19]  O. Witte,et al.  The BCR gene encodes a novel serine/threonine kinase activity within a single exon , 1991, Cell.

[20]  D. Mochly‐Rosen,et al.  Intracellular receptors for activated protein kinase C. Identification of a binding site for the enzyme. , 1991, The Journal of biological chemistry.

[21]  O. Witte,et al.  BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner , 1991, Cell.

[22]  C. Hall,et al.  Bcr encodes a GTPase-activating protein for p21rac , 1991, Nature.

[23]  D. Mochly‐Rosen,et al.  Identification of intracellular receptor proteins for activated protein kinase C. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[24]  O. Witte,et al.  BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias , 1991, Molecular and cellular biology.

[25]  P. Nielsen.  Primary structure of a human protein kinase regulator protein. , 1991, Biochimica et biophysica acta.

[26]  J. Wang,et al.  Activation of tyrosinase kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins , 1991, Molecular and cellular biology.

[27]  T. Hunter,et al.  Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. , 1991, Methods in enzymology.

[28]  W. Herr,et al.  Differential transcriptional activation by Oct-1 and Oct-2: Interdependent activation domains induce Oct-2 phosphorylation , 1990, Cell.

[29]  S. Smith,et al.  Expression of a distinctive BCR-ABL oncogene in Ph1-positive acute lymphocytic leukemia (ALL). , 1988, Science.

[30]  N. Heisterkamp,et al.  Unique fusion of bcr and c-abl genes in Philadelphia chromosome positive acute lymphoblastic leukemia , 1987, Cell.

[31]  G. Daley,et al.  The chronic myelogenous leukemia-specific P210 protein is the product of the bcr/abl hybrid gene. , 1986, Science.

[32]  E. Canaani,et al.  Fused transcript of abl and bcr genes in chronic myelogenous leukaemia , 1985, Nature.

[33]  J. Stephenson,et al.  Philadelphia chromosomal breakpoints are clustered within a limited region, bcr, on chromosome 22 , 1984, Cell.

[34]  J. Stephenson,et al.  Localization of the c-abl oncogene adjacent to a translocation break point in chronic myelocytic leukaemia , 1983, Nature.