Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.5.1.18 (glutathione S-transferase)
 22,582 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

TATA-binding protein (TBP) forms complexes with various nuclear proteins and plays roles in all eukaryotic transcription. We previously identified TBP-interacting protein 120 (TIP120) from rat liver. TIP120 stimulates in vitro transcription generally. Homologs of TIP120 exist in various higher eukaryotes including D. melanogaster, C. elegans, and A. thaliana. Here, we isolated cDNA of a novel rat TIP120-like protein, named TIP120B. Rat TIP120B was composed of 1,235 amino acids and was 60% identical to the original TIP120 (re-named TIP120A). However, TIP120B gene was expressed specifically in the muscle tissues, which was contrary to the ubiquitous expression of TIP120A. Moreover, TIP120B protein was observed exclusively in the muscle tissues. TIP120B is therefore suggested to be a muscle-specific protein. Northern blot analysis of the mouse embryo revealed that the expression of TIP120B was temporarily increased during the embryogenesis, whereas TIP120A maintained a constant expression level. Pull-down assay using GST-fused TBP demonstrated that TBP specifically associated with TIP120B in the nuclear extract. These results indicate that TIP120B is a muscle-specific TIP120 family protein and can also interact with TBP. TIP120B is supposed to have a specific role in muscle tissues, which may be diffrerent from that of TIP120A.
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PMID:TIP120B: a novel TIP120-family protein that is expressed specifically in muscle tissues. 1044 24

TBP-interacting protein 120 (TIP120) has been identified by TBP-mediated affinity screening. Classical TIP120, TIP120A, which functions as a transcriptional activator, is expressed ubiquitously whereas TIP120B is specifically expressed in muscle tissues. We found that TIP120B gene was induced in C2C12 myoblasts when these cells differentiated into myotubes, whereas TIP120A gene expression was down-regulated. Whole-mount in situ hybridization revealed that TIP120B mRNA was concentrated in limb buds of mouse embryos. TIP120B is thus thought to be a myogenesis-responding gene. We searched for TIP120B-binding proteins by yeast two-hybrid screening and identified NOT3. NOT3, a constituent of CCR4-NOT complex, is suggested to be involved in global gene regulation via interaction with TBP. The human NOT3 (hNOT3L), which we identified, has an extra 144 amino acids (AAs) at the C-terminus of a classical NOT3. GST pull-down and yeast two-hybrid assays demonstrated that hNOT3L is associated with TIP120B but not with TIP120A. A hNOT3L-specific C-terminal region of 92 AAs was assigned as a TIP120B-interacting domain. The N-terminus of 209 AAs of TIP120B was responsible for this binding. TIP120B presumably affects tissue-specific transcriptional regulation via interaction with NOT3.
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PMID:TBP-interacting protein 120B, which is induced in relation to myogenesis, binds to NOT3. 1220 86

The molecular mechanism involved in the exocytosis of arginine vasopressin (AVP) is not fully known. Rabphilin-3A has been suggested as a novel autoantigen in infundibulo-neurohypophysitis (LINH), which leads to central diabetes insipidus through insufficient secretion of AVP. However, the role of rabphilin-3A in the pathogenesis of LINH remains unclear. Thus, the aim of the present study was to identify proteins binding rabphilin-3A in the posterior pituitary. Using glutathione S-transferase (GST)-pulldown assays and proteomic analyses, cullin-associated NEDD8-dissociated protein 1 (CAND1) was identified as a rabphilin-3A-binding protein in the posterior pituitary. Co-immunoprecipitation assays indicated that CAND1 interacted endogenously with rabphilin-3A. In addition, immunohistochemistry experiments showed that CAND1 immunoreactivity was detected mainly in the posterior pituitary, intermediate lobe, and the supraoptic nucleus in the hypothalamus, and less in the anterior lobe, partially co-localizing with rabphilin-3A. Overexpression of CAND1 resulted in deubiquitylation of rabphilin-3A in PC12 cells. Moreover, overexpression of CAND1 in PC12 cells co-transfected with AVP enhanced both basal and KCl-stimulated AVP secretion. The findings indicate that CAND1 inhibits the ubiquitylation of rabphilin-3A and positively regulates AVP secretion. These data shed light on a novel potential mechanism involving rabphilin-3A in AVP secretion, and suggest a new role of CAND1 as a regulator of hormone or neurotransmitter secretion.
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PMID:Cullin-associated NEDD8-dissociated protein 1, a novel interactor of rabphilin-3A, deubiquitylates rabphilin-3A and regulates arginine vasopressin secretion in PC12 cells. 2936 74