A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette.

Walden, Paul D.; Cowan, Nicholas J.

doi:10.1128/mcb.13.12.7625

Cited by 72 publications

(68 citation statements)

References 46 publications

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“…In addition, the N-terminal half of the small leucine zipper-containing protein B3-1 ] is comprised of a DHR motif. Finally, and most interestingly, we identified a single DHR motif in the testis-specific serine/ threonine kinase MAST205 [Walden and Cowan, 1993]. MAST205 can associate to MAP-coated microtubules and this binding is displayed by a small protein segment just downstream of the kinase domain.…”

Section: Discussionmentioning

confidence: 83%

Molecular cloning of a mouse epithelial protein‐tyrosine phosphatase with similarities to submembranous proteins

Hendriks

Schepens

Bächner

et al. 1995

J of Cellular Biochemistry

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Protein-tyrosine phosphatases (PTPases) form an important class of cell regulatory proteins. We have isolated overlapping cDNA clones that together comprise an 8 kb transcript encoding a novel murine PTPase which is expressed in various organs. Sequence analysis revealed an open reading frame of 2,460 amino acid residues. The predicted protein, PTP-BL, is a large non-transmembrane PTPase that exhibits 80% homology with PTP-BAS, a recently described human PTPase. PTP-BL shares some intriguing sequence homologies with submembranous proteins. It contains a band 4.1 -like motif also present in the tumor suppressors neurofibromatosis 2 and expanded, five 80 amino acid repeats also present in the discs-large tumor suppressor, and a single catalytic phosphatase domain. No obvious homologies to other proteins were found for the N-terminal region of the protein other than human PTP-BAS. RNA in situ hybridization experiments show that the PTP-BL gene is expressed in epithelial cells, predominantly in kidney, lung, and skin. These data suggest a cell cortical localization for PTP-BL in epithelial cells and a possible role in the morphology and motility of epithelial tissues.

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Section: Discussionmentioning

confidence: 83%

Molecular cloning of a mouse epithelial protein‐tyrosine phosphatase with similarities to submembranous proteins

Hendriks

Schepens

Bächner

et al. 1995

J of Cellular Biochemistry

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“…␤-Actin was visualized by phalloidin-Texas Red. Anti MAST205 antibody was kindly provided by P. Walden (31), and an anti-HSP86 antibody was purchased from Affinity Purified Reagents.…”

Section: Gst Fusion Constructs and Protein Expression-mentioning

confidence: 99%

Interaction of the Type IIa Na/Pi Cotransporter with PDZ Proteins

Gisler¹,

Štagljar²,

Traebert

et al. 2001

Journal of Biological Chemistry

228

285

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The type IIa Na ؉ -dependent inorganic phosphate (Na/ P i ) cotransporter is localized in the apical membrane of proximal tubular cells and is regulated by an endocytotic pathway. Because molecular processes such as apical sorting, internalization, or subsequent degradation might be assisted by associated proteins, a yeast twohybrid screen against the C-terminal, cytosolic tail of type IIa cotransporter was designed. Most of the potential proteins found belonged to proteins with multiple PDZ modules and were either identical/related to PDZK1 or identical to NHERF-1. Yeast trap truncation assays confined the peptide-protein association to the C-terminal amino acid residues TRL of type IIa cotransporter and to single PDZ domains of each identified protein, respectively. The specificity of these interactions were confirmed in yeast by testing other apical localized transmembraneous proteins. Moreover, the type IIa protein was recovered in vitro by glutathione S-transferase-fused PDZ proteins from isolated renal brush border membranes or from type IIa-expressing oocytes. Further, these PDZ proteins are immunohistochemically detected either in the microvilli or in the subapical compartment of proximal tubular cells. Our results suggest that the type IIa Na/P i cotransporter interacts with various PDZ proteins that might be responsible for the apical sorting, parathyroid hormone controlled endocytosis or the lysosomal sorting of internalized type IIa cotransporter.In kidney, reabsorption of filtered inorganic phosphate (P i ) takes place along the proximal tubules and is controlled by a variety of hormones (e.g. parathyroid hormone, PTH) 1 and other factors (e.g. dietary intake of P i ) (1, 2). Three structurally unrelated sodium-dependent phosphate (Na/P i ) cotransporter families have been identified (1, 3). By immunohistochemistry, it was apparent that members of the type I and the type IIa Na/P i cotransporters are located in the apical membrane of proximal tubular cells (4, 5). Targeted inactivation of the type IIa Na/P i cotransporter gene (npt2) provided strong evidence that ϳ70% of Na-dependent P i transport across the brush border membrane is mediated by the type IIa Na/P i cotransporter (6). Furthermore, the type IIa cotransporter represents the major target for the many factors described to regulate proximal tubular P i reabsorption (2). Additionally, reduced proximal P i -reabsorption, as observed in X-linked hypophosphatemia, is due to a decreased abundance of the type IIa Na/P i cotransporter (7).According to the current mechanistic view, inhibition of proximal tubular Pi-reabsorption, such as by PTH or by a diet of high P i content (acutely given), is achieved by a removal of type IIa cotransporters (2) from the apical membrane. Results obtained from in vivo (rats) and in vitro (OK cells) studies indicated that internalized type IIa Na/P i cotransporters are subjected to degradation in the lysosomes (8, 9). Besides Na/P i cotransport, the activity of the brush border Na/H exchanger, NHE-3, is regulated ...

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“…: 212-659-9402; Fax: 212-849-2525; E-mail: jay.unkeless@mssm.edu. 1 The abbreviations used are: MAST205, microtubule-associated serine/threonine kinase, 205 kDa; LPS, lipopolysaccharide; DN, dominant negative; Fc␥R, Fc␥ receptor; HA, hemagglutinin; IKK, I 〉 kinase; MG132, carbobenzoxy-Leu-Leu-Leu-al; PDZ, postsynaptic density protein-95, discs large protein, zonula occludens; PEST, proline, glutamine, serine, threonine rich sequences, proline, glutamine; RNAi, RNA interference; TLR, toll-like receptor; TPCK, N-p-tosyl-L-phenylalanine chloromethyl ketone; IL, interleukin; E2, ubiquitin carrier protein; E3 ubiquitin-protein isopeptide ligase; mAb, monoclonal antibody; CMV, cytomegalovirus.…”

mentioning

confidence: 99%

“…At neuromuscular synapses MAST205 interacts with ␤-2 syntrophin (1,2). In addition to a well conserved protein kinase C/A kinase domain, MAST205 has a PDZ domain, a protein-protein recognition module (3).…”

mentioning

confidence: 99%

Interaction of TRAF6 with MAST205 Regulates NF-κB Activation and MAST205 Stability

Xiong

Chen

et al. 2004

Journal of Biological Chemistry

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The binding of immune complexes to macrophage Fc␥ receptor results in a subsequent inhibition of lipopolysaccharide-stimulated interleukin-12 synthesis without affecting the induction of tumor necrosis factor-␣. RNA interference targeting MAST205, a 205-kDa serine/ threonine kinase, and transfection of dominant negative MAST205 mutants also mimic this type II macrophage phenotype. Our previous epistasis experiments suggested that the position of MAST205 in the TLR4 signal pathway was proximal to the I B kinase complex. We now report that MAST205 forms a complex with TRAF6, resulting in the inhibition of TRAF6 NF-B activation. We have identified a peptide (residues 218 -233) from the N terminus of MAST205 that, when coupled to a protein transduction domain, inhibits the lipopolysaccharidestimulated activation of NF-B, modulates the size of the MAST205⅐TRAF6 complex, and inhibits ubiquitination of TRAF6. A dominant negative N-terminal MAST205 deletion mutant also inhibits TRAF6 ubiquitination. The domain required for degradation of MAST205 after Fc␥ receptor activation resides within the N-terminal 261 residues, and degradation is triggered by protein kinase C isoform phosphorylation of Ser/Thr residues. These results suggest that MAST205 functions as a scaffolding protein controlling TRAF6 activity and, therefore, plays an important role in regulating inflammatory responses.MAST205 1 is a 205-kDa Ser/Thr kinase that is widely expressed at low levels and highly expressed in spermatids, where MAST205 associates with microtubules. At neuromuscular synapses MAST205 interacts with ␤-2 syntrophin (1, 2). In addition to a well conserved protein kinase C/A kinase domain, MAST205 has a PDZ domain, a protein-protein recognition module (3). The role of MAST205 in cellular physiology, however, has yet to be determined. We have found that MAST205 plays a central role in the regulation of LPS-induced cytokine responses of macrophages (4). In this paper we analyze in greater detail the position of MAST205 in LPS-induced signal pathways and the factors regulating stability of the protein.Macrophages respond to LPS by secreting proinflammatory cytokines such as tumor necrosis factor-␣, IL-1, IL-6, IL-8, and IL-12. IL-12, in particular, is required for the induction of a T helper 1 response that facilitates the clearance of intracellular pathogens. The signal cascade leading to the inflammatory response is complex, reflecting both the importance of controlling the synthesis of potentially harmful cytokines and metabolites, such as reactive oxygen intermediates, and the need to tailor the response depending on the pathogen (5). The inflammatory response is also influenced by previous physiological stimuli to the responding cells, which has lent credence to the concept of macrophage subsets. For example, LPS-stimulated synthesis of IL-12 by macrophages, which is required for the induction of interferon-␥ from NK cells (6), is inhibited by immune complex activation of Fc␥R. As a result, such type II macrophages (7) as antigen present...

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A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette.

Cited by 72 publications

References 46 publications

Molecular cloning of a mouse epithelial protein‐tyrosine phosphatase with similarities to submembranous proteins

Molecular cloning of a mouse epithelial protein‐tyrosine phosphatase with similarities to submembranous proteins

Interaction of the Type IIa Na/Pi Cotransporter with PDZ Proteins

Interaction of TRAF6 with MAST205 Regulates NF-κB Activation and MAST205 Stability

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