This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ziegler, S F Articles by Perlmutter, R M Search for Related Content PubMed PubMed Citation Articles by Ziegler, S F Articles by Perlmutter, R M

 Previous Article  |  Next Article 

Mol Cell Biol. 1987 June; 7(6): 2276-2285

Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin.

ABSTRACT

Protein-tyrosine kinases are implicated in the control of cell growth by virtue of their frequent appearance as products of retroviral oncogenes and as components of growth factor receptors. Here we report the characterization of a novel human protein-tyrosine kinase gene (hck) that is primarily expressed in hematopoietic cells, particularly granulocytes. The hck gene encodes a 505-residue polypeptide that is closely related to pp56lck, a lymphocyte-specific protein-tyrosine kinase. The exon breakpoints of the hck gene, partially defined by using murine genomic clones, demonstrate that hck is a member of the src gene family and has been subjected to strong selection pressure during mammalian evolution. High-level expression of hck transcripts in granulocytes is especially provocative since these cells are terminally differentiated and typically survive in vivo for only a few hours. Thus the hck gene, like other members of the src gene family, appears to function primarily in cells with little growth potential.

This article has been cited by other articles:

• Trible, R. P., Emert-Sedlak, L., Smithgall, T. E. (2006). HIV-1 Nef Selectively Activates Src Family Kinases Hck, Lyn, and c-Src through Direct SH3 Domain Interaction. J. Biol. Chem. 281: 27029-27038 [Abstract] [Full Text]  
• Ling, S., Sheng, J.-Z., Braun, A. P. (2004). The calcium-dependent activity of large-conductance, calcium-activated K+ channels is enhanced by Pyk2- and Hck-induced tyrosine phosphorylation. Am. J. Physiol. Cell Physiol. 287: C698-C706 [Abstract] [Full Text]  
• Podar, K., Mostoslavsky, G., Sattler, M., Tai, Y.-T., Hayashi, T., Catley, L. P., Hideshima, T., Mulligan, R. C., Chauhan, D., Anderson, K. C. (2004). Critical Role for Hematopoietic Cell Kinase (Hck)-mediated Phosphorylation of Gab1 and Gab2 Docking Proteins in Interleukin 6-induced Proliferation and Survival of Multiple Myeloma Cells. J. Biol. Chem. 279: 21658-21665 [Abstract] [Full Text]  
• Shivakrupa, R., Radha, V., Sudhakar, Ch., Swarup, G. (2003). Physical and Functional Interaction between Hck Tyrosine Kinase and Guanine Nucleotide Exchange Factor C3G Results in Apoptosis, Which Is Independent of C3G Catalytic Domain. J. Biol. Chem. 278: 52188-52194 [Abstract] [Full Text]  
• Lee, S., Lin, X., Nam, N. H., Parang, K., Sun, G. (2003). Determination of the substrate-docking site of protein tyrosine kinase C-terminal Src kinase. Proc. Natl. Acad. Sci. USA 100: 14707-14712 [Abstract] [Full Text]  
• Yokoyama, N., Miller, W. T. (2003). Biochemical Properties of the Cdc42-associated Tyrosine Kinase ACK1: SUBSTRATE SPECIFICITY, AUTOPHOSPHORYLATION, AND INTERACTION WITH Hck. J. Biol. Chem. 278: 47713-47723 [Abstract] [Full Text]  
• Carter, K. L., Cahir-McFarland, E., Kieff, E. (2002). Epstein-Barr Virus-Induced Changes in B-Lymphocyte Gene Expression. J. Virol. 76: 10427-10436 [Abstract] [Full Text]  
• Scott, M. P., Zappacosta, F., Kim, E. Y., Annan, R. S., Miller, W. T. (2002). Identification of Novel SH3 Domain Ligands for the Src Family Kinase Hck. WISKOTT-ALDRICH SYNDROME PROTEIN (WASP), WASP-INTERACTING PROTEIN (WIP), AND ELMO1. J. Biol. Chem. 277: 28238-28246 [Abstract] [Full Text]  
• Gottlieb, K. A., Villarreal, L. P. (2001). Natural Biology of Polyomavirus Middle T Antigen. Microbiol. Mol. Biol. Rev. 65: 288-318 [Abstract] [Full Text]  
• Scholz, G., Hartson, S. D., Cartledge, K., Hall, N., Shao, J., Dunn, A. R., Matts, R. L. (2000). p50Cdc37 Can Buffer the Temperature-Sensitive Properties of a Mutant of Hck. Mol. Cell. Biol. 20: 6984-6995 [Abstract] [Full Text]  
• Foti, M., Cartier, L., Piguet, V., Lew, D. P., Carpentier, J.-L., Trono, D., Krause, K.-H. (1999). The HIV Nef Protein Alters Ca2+ Signaling in Myelomonocytic Cells through SH3-mediated Protein-Protein Interactions. J. Biol. Chem. 274: 34765-34772 [Abstract] [Full Text]  
• Briggs, S. D., Smithgall, T. E. (1999). SH2-Kinase Linker Mutations Release Hck Tyrosine Kinase and Transforming Activities in Rat-2 Fibroblasts. J. Biol. Chem. 274: 26579-26583 [Abstract] [Full Text]  
• Hauses, M., Tonjes, R. R., Grez, M. (1998). The Transcription Factor Sp1 Regulates the Myeloid-specific Expression of the Human Hematopoietic Cell Kinase (HCK) Gene through Binding to Two Adjacent GC Boxes within the HCK Promoter-Proximal Region. J. Biol. Chem. 273: 31844-31852 [Abstract] [Full Text]  
• LaFevre-Bernt, M., Sicheri, F., Pico, A., Porter, M., Kuriyan, J., Miller, W. T. (1998). Intramolecular Regulatory Interactions in the Src Family Kinase Hck Probed by Mutagenesis of a Conserved Tryptophan Residue. J. Biol. Chem. 273: 32129-32134 [Abstract] [Full Text]  
• Itoh, K., Okubo, K., Utiyama, H., Hirano, T., Yoshii, J., Matsubara, K. (1998). Expression Profile of Active Genes in Granulocytes. Blood 92: 1432-1441 [Abstract] [Full Text]  
• Jones, A. E., Saksela, K., Game, S. M., O'Beirne, G., Cook, N. D. (1998). Screening Assay for the Detection of the Protein-Protein Interaction Between HIV-1 Nef Protein and the SH3 Domain of Hck. J Biomol Screen 3: 37-41 [Abstract]  
• Gulle, H., Samstag, A., Eibl, M. M., Wolf, H. M. (1998). Physical and Functional Association of Fcalpha R With Protein Tyrosine Kinase Lyn. Blood 91: 383-391 [Abstract] [Full Text]  
• Briggs, S. D., Sharkey, M., Stevenson, M., Smithgall, T. E. (1997). SH3-mediated Hck Tyrosine Kinase Activation and Fibroblast Transformation by the Nef Protein of HIV-1. J. Biol. Chem. 272: 17899-17902 [Abstract] [Full Text]  
• Welch, H., Maridonneau-Parini, I. (1997). Hck Is Activated by Opsonized Zymosan and A23187 in Distinct Subcellular Fractions of Human Granulocytes. J. Biol. Chem. 272: 102-109 [Abstract] [Full Text]  
• Brumell, J. H., Burkhardt, A. L., Bolen, J. B., Grinstein, S. (1996). Endogenous Reactive Oxygen Intermediates Activate Tyrosine Kinases in Human Neutrophils. J. Biol. Chem. 271: 1455-1461 [Abstract] [Full Text]  
• Briggs, S. D., Bryant, S. S., Jove, R., Sanderson, S. D., Smithgall, T. E. (1995). The Ras GTPase-activating Protein (GAP) Is an SH3 Domain-binding Protein and Substrate for the Src-related Tyrosine Kinase, Hck. J. Biol. Chem. 270: 14718-14724 [Abstract] [Full Text]  
• Lowell, C A, Soriano, P, Varmus, H E (1994). Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity.. Genes Dev. 8: 387-398 [Abstract]  
• Koch, C., Anderson, D, Moran, M., Ellis, C, Pawson, T (1991). SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252: 668-674 [Abstract]  
• Hirai, H, Varmus, H E (1990). SH2 mutants of c-src that are host dependent for transformation are trans-dominant inhibitors of mouse cell transformation by activated c-src.. Genes Dev. 4: 2342-2352 [Abstract]  
• Dymecki, S., Niederhuber, J., Desiderio, S. (1990). Specific expression of a tyrosine kinase gene, blk, in B lymphoid cells. Science 247: 332-336 [Abstract]  
• Hanks, S., Quinn, A., Hunter, T (1988). The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241: 42-52 [Abstract]  
• Verkoczy, L. K., Guinn, B.-a., Berinstein, N. L. (2000). Characterization of the Human B Cell RAG-associated Gene, hBRAG, as a B Cell Receptor Signal-enhancing Glycoprotein Dimer That Associates with Phosphorylated Proteins in Resting B Cells. J. Biol. Chem. 275: 20967-20979 [Abstract] [Full Text]  
• Carreno, S., Gouze, M.-E., Schaak, S., Emorine, L. J., Maridonneau-Parini, I. (2000). Lack of Palmitoylation Redirects p59Hck from the Plasma Membrane to p61Hck-positive Lysosomes. J. Biol. Chem. 275: 36223-36229 [Abstract] [Full Text]  
• Briggs, S. D., Scholtz, B., Jacque, J.-M., Swingler, S., Stevenson, M., Smithgall, T. E. (2001). HIV-1 Nef Promotes Survival of Myeloid Cells by a Stat3-dependent Pathway. J. Biol. Chem. 276: 25605-25611 [Abstract] [Full Text]  
• Zilber, M.-T., Gregory, S., Mallone, R., Deaglio, S., Malavasi, F., Charron, D., Gelin, C. (2000). CD38 expressed on human monocytes: A coaccessory molecule in the superantigen-induced proliferation. Proc. Natl. Acad. Sci. USA 97: 2840-2845 [Abstract] [Full Text]