A Protein Kinase Cδ-binding Protein SRBC Whose Expression Is Induced by Serum Starvation

Izumi, Yasushi; Hirai, Syu-ichi; Tamai, Yoko; Fujise-Matsuoka, Ariko; Nishimura, Yoshifumi; Ohno, Shigeo

doi:10.1074/jbc.272.11.7381

Cited by 91 publications

(106 citation statements)

References 35 publications

(40 reference statements)

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“…Five of these genes were analysed by Northern blotting. The greatest difference in expression (five-fold higher in R þ cells) was observed with PKCd-binding protein (Izumi et al, 1997) (Figure 3). Low Molecular Weight-Protein Tyrosine Phosphatase (Lmw-ptp), which can negatively regulate growth (Fiaschi et al, 2001), was expressed almost four-fold more in R þ cells (Figure 3).…”

Section: Resultsmentioning

confidence: 97%

Gene expression profiles in cells transformed by overexpression of the IGF-I receptor

et al. 2005

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To identify genes associated with insulin-like growth factor-I receptor (IGF-IR)-mediated cellular transformation, we isolated genes that are differentially expressed in R À cells (derived from the IGF-IR knockout mouse) and R þ cells (R À cells that overexpress the IGF-IR). From these, 45 genes of known function were expressed at higher levels in R þ cells and 22 were expressed at higher levels in R À cells. Differential expression was confirmed by Northern blot analysis of R þ and R À cells. Genes expressed more abundantly in R þ cells are associated with (1) tumour growth and metastasis including, bigH3, mts1, igfbp5 protease, and mystique; (2) cell division, including cyclin A1 and cdk1; (3) signal transduction, including pkcdbp and lmw-ptp; and (4) metabolism including ATPase H þ transporter and ferritin. In MCF-7 cells IGF-I induced expression of two genes, lasp-1 and mystique, which could contribute to metastasis. Lasp-1 expression required activity of the PI3-kinase signalling pathway. Mystique was highly expressed in metastatic but not in androgen-dependent prostate cancer cell lines and Mystique overexpression in MCF-7 cells promoted cell migration and invasion. We conclude that genes identified in this screen may mediate IGF-IR function in cancer progression.

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Section: Resultsmentioning

confidence: 97%

Gene expression profiles in cells transformed by overexpression of the IGF-I receptor

et al. 2005

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“…cDNAs-Rat p20 and human HSPB3 cDNAs were amplified from a rat 3Y1 cell cDNA library (29) and a human skeletal muscle cDNA library (CLONTECH Laboratories, Inc., Palo Alto, CA), respectively, by PCR using appropriate synthetic oligonucleotide primers flanking the ORF of each protein. The preparation of the cDNAs for MKBP/HSPB2, ␣B-crystallin, and HSP27 has been described previously (23).…”

Section: Methodsmentioning

confidence: 99%

Muscle Develops a Specific Form of Small Heat Shock Protein Complex Composed of MKBP/HSPB2 and HSPB3 during Myogenic Differentiation

Sugiyama

Suzuki

Kishikawa

et al. 2000

Journal of Biological Chemistry

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Previously, we identified a new mammalian sHSP, MKBP, as a myotonic dystrophy protein kinase-binding protein, and suggested its important role in muscle maintenance (Suzuki, A., Sugiyama, Y., Hayashi, Y., Nyu-i, N., Yoshida, M., Nonaka, I., Ishiura, S., Arahata, K., and Ohno, S. (1998) J. Cell Biol. 140, 1113-1124). In this paper, we develop the former work by performing extensive characterization of five of the six sHSPs so far identified, that is, HSP27, ␣B-crystallin, p20, MKBP/ HSPB2, and HSPB3, omitting lens-specific ␣A-crystallin. Tissue distribution analysis revealed that although each sHSP shows differential constitutive expression in restricted tissues, tissues that express all five sHSPs are only muscle-related tissues. Especially, the expressions of HSPB3, identified for the first time as a 17-kDa protein in this paper, and MKBP/HSPB2 are distinctly specific to muscles. Moreover, these sHSPs form an oligomeric complex with an apparent molecular mass of 150 kDa that is completely independent of the oligomers formed by HSP27, ␣B-crystallin, and p20. The expressions of MKBP/HSPB2 and HSPB3 are induced during muscle differentiation under the control of MyoD, suggesting that the sHSP oligomer comprising MKBP/ HSPB2 and HSPB3 represents an additional system closely related to muscle function. The functional divergence among sHSPs in different oligomers is also demonstrated in several ways: 1) an interaction with myotonic dystrophy protein kinase, which has been suggested to be important for the maintenance of myofibril integrity, was observed only for MKBP/HSPB2; 2) a myotube-specific association with actin bundles was observed for HSP27 and ␣B-crystallin, but not for MKBP/ HSPB2; and 3) sHSPs whose mRNAs are induced by heat shock are ␣B-crystallin and HSP27. Taken together, the results suggest that muscle cells develop two kinds of stress response systems composed of diverged sHSP members, and that these systems work independently in muscle maintenance and differentiation.Heat shock and numerous other stress conditions lead to the rapid induction of several genes whose protein products, collectively called heat shock proteins (HSPs), 1 play protective roles in cell survival (1). Considering that muscles are frequently subjected to severe conditions caused by heat, oxidative, and mechanical stresses, especially during exercise (2), these HSPs may be especially important in this particular tissue. In fact, several HSPs, including HSP60, 70, and 90, have been shown to be induced after exhaustive exercise (3). In addition, the inducible isoform of HSP70 has been shown to be constitutively expressed in a certain type of skeletal muscle fiber (4), suggesting that muscle cells are chronically ready to respond to frequent stresses. However, there have been limited numbers of studies that focus on HSPs in muscle cells.HSPs with low molecular masses of 15-30 kDa are called small heat shock proteins (sHSPs); they commonly share a homologous sequence of about 80 amino acids called the "␣-crystallin domain" (5). Among ...

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“…Baculovirus-infected Insect Cells-In vitro transcription/translation of the DIK cDNA in a rabbit reticulocyte lysate system resulted in the synthesis of several forms of the DIK protein with apparent molecular masses ranging from around 95 to 106 kDa, as demonstrated by SDS-PAGE and autoradiography of the 35 S-labeled proteins (Fig. 4A).…”

Section: Pression Of Recombinant Dik In Bacteria Hek Cells Andmentioning

confidence: 99%

“…A, the reticulocyte lysates were incubated with the vector pGEM3Z alone (left lane) or with pGEM3Z/DIK (right lane) as described under "Experimental Procedures" and analyzed by SDS-PAGE. In vitro synthesized 35 S-labeled proteins were visualized by autoradiography. B, bacteria were transfected with pGEX (vector control) or pGEX/DIK ("Experimental Procedures").…”

Section: Pression Of Recombinant Dik In Bacteria Hek Cells Andmentioning

confidence: 99%

DIK, a Novel Protein Kinase That Interacts with Protein Kinase Cδ

Bähr

Rohwer

Stempka

et al. 2000

Journal of Biological Chemistry

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A novel serine/threonine kinase, termed DIK, was cloned using the yeast two-hybrid system to screen a cDNA library from the human keratinocyte cell line HaCaT with the catalytic domain of rat protein kinase C␦ (PKC␦ cat ) cDNA as bait. The predicted 784-amino acid polypeptide with a calculated molecular mass of 86 kDa contains a catalytic kinase domain and a putative regulatory domain with ankyrin-like repeats and a nuclear localization signal. Expression of DIK at the mRNA and protein level could be demonstrated in several cell lines. The dik gene is located on chromosome 21q22.3 and possesses 8 exons and 7 introns. DIK was synthesized in an in vitro transcription/translation system and expressed as recombinant protein in bacteria, HEK, COS-7, and baculovirus-infected insect cells. In the in vitro system and in cells, but not in bacteria, various post-translationally modified forms of DIK were produced. DIK was shown to exhibit protein kinase activity toward autophosphorylation and substrate phosphorylation. The interaction of PKC␦ cat and PKC␦ with DIK was confirmed by coimmunoprecipitation of the proteins from HEK cells transiently transfected with PKC␦ cat or PKC␦ and DIK expression constructs.The members of the PKC 1 family, because of structural and enzymatic differences, can be subdivided into several groups (for reviews see Refs. 1 and 2). PKC␦, a member of the so-called nPKC subfamily, has attracted the interest of an increasing number of research groups over the last years and presumably is one of the most thoroughly studied PKC isoenzymes (for a review see Ref. 3). Like all the other PKC isoforms, PKC␦ is thought to play an individual role in various signaling pathways and to specifically affect diverse cellular processes, such as growth, differentiation, apoptosis, and tumorigenesis (4 -16). This specific action is likely to afford a sophisticated network of regulation of PKC␦ activity, subcellular localization, and substrate phosphorylation. Beside the well known regulation of enzyme activity by signal-induced second messengers, such as diacylglycerol, PKC␦ is regulated by up-and downmodulation of its expression (4, 17, 18), by phosphorylation (19 -29), and presumably by interaction with other proteins involved in signal transduction, such as other protein kinases and anchor or docking proteins (30 -38). Particularly the latter is essential for a specific subcellular localization of the enzyme and a selective phosphorylation of substrate proteins. Our knowledge of PKC␦-protein interactions, however, is rather scanty. This holds true not only for the interaction with physiologically relevant substrate proteins but also for the interaction with other proteins that might affect PKC␦ signaling.We therefore attempted to clone proteins interacting with PKC␦ by using the yeast two-hybrid system (YTHS). Here, we describe the cloning, expression, and characterization of a novel serine/threonine kinase, termed DIK (PKC-delta-interacting protein kinase), which is coimmunoprecipitated with PKC␦ and the catalyti...

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A Protein Kinase Cδ-binding Protein SRBC Whose Expression Is Induced by Serum Starvation

Cited by 91 publications

References 35 publications

Gene expression profiles in cells transformed by overexpression of the IGF-I receptor

Gene expression profiles in cells transformed by overexpression of the IGF-I receptor

Muscle Develops a Specific Form of Small Heat Shock Protein Complex Composed of MKBP/HSPB2 and HSPB3 during Myogenic Differentiation

DIK, a Novel Protein Kinase That Interacts with Protein Kinase Cδ

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