BAG4/SODD Protein Contains a Short BAG Domain

Briknarová, Klára; Takayama, Shinichi; Homma, Sachiko; Baker, Kelly K.; Cabezas, Edelmira; Hoyt, David; Li, Zhen; Satterthwait, Arnold C.; Ely, Kathryn R.

doi:10.1074/jbc.m202792200

Cited by 54 publications

(48 citation statements)

References 26 publications

(45 reference statements)

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“…Structure determination by solution NMR showed a bundle of three antiparallel-helices, of which helices 2 and 3 interact with the ATPase domain of DnaK [167]. Subsequent structure determination of different members of the Bag family revealed a conserved three-helix bundle, whereas these proteins showed significant differences in the length of the respective helices and their charge distributions [168,169].…”

Section: Dnakmentioning

confidence: 99%

Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists

Burmann¹,

Hiller²

2015

Progress in Nuclear Magnetic Resonance Spectroscopy

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Section: Dnakmentioning

confidence: 99%

Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists

Burmann¹,

Hiller²

2015

Progress in Nuclear Magnetic Resonance Spectroscopy

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“…M AMMALIAN Bcl1-associated athanogene (BAG)-domain proteins, named after the founding member BAG-1 (Takayama et al 1995), are Hsp70-family cochaperones implicated in cell survival, intracellular signaling, gene expression, and human disorders such as Parkinson's disease (Takayama et al 1995(Takayama et al , 1997(Takayama et al , 1999Gebauer et al 1997;Hö hfeld and Jentsch 1997;Zeiner et al 1997;Liu et al 1998;Antoku et al 2001;Briknarova et al 2002;Kalia et al 2004;reviewed in Doong et al 2002;Alberti et al 2003;Gehring 2004;Townsend et al 2005). The 80-amino-acid C-terminal BAG domain comprises an antiparallel, amphipathic, three-helix bundle structure (Briknarova et al 2001;Sondermann et al 2001;Brockmann et al 2004;Symersky et al 2004), which interacts with the ATPase domain of Hsc70 and Hsp70 (Hö hfeld and Jentsch 1997; Takayama et al 1997).…”

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confidence: 99%

Drosophila starvin Encodes a Tissue-Specific BAG-Domain Protein Required for Larval Food Uptake

2005

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We describe a developmental, genetic, and molecular analysis of the sole Drosophila member of the BAG family of genes, which is implicated in stress response and survival in mammalian cells. We show that the gene, termed starvin (stv), is expressed in a highly tissue-specific manner, accumulating primarily in tendon cells following germ-band retraction and later in somatic muscles and the esophagus during embryonic stage 15. We show that stv expression falls within known tendon and muscle cell transcriptional regulatory cascades, being downstream of stripe, but not of another tendon transcriptional regulator, delilah, and downstream of the muscle regulator, mef-2. We generated a series of stv alleles and, surprisingly, given the muscle and tendon-specific embryonic expression of stv, found that the gross morphology and function of somatic muscles is normal in stv mutants. Nonetheless, stv mutant larvae exhibit a striking and fully penetrant mutant phenotype of failure to grow after hatching and a severely impaired ability to take up food. Our study provides the first report of an essential, developmentally regulated BAG-family gene.

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“…SODD contains a sequence closely associated with cytotoxic activity, i.e., the DD. SODD exerts its biological function through its specific binding with DDs in the cytoplasmic regions of TNFR-I, Bcl-2, DR3, and HSP/HSC70 (Briknarová et al, 2002). SODD integrates with the DD of TNFR-I to form an SODD-TNFR-I complex for the prevention of TNFR-I aggregation and the disruption of the TNFR-I signaling pathway.…”

Section: Discussionmentioning

confidence: 99%

Significance of SODD expression in childhood acute lymphoblastic leukemia and its influence on chemotherapy

Tao¹,

Liu²,

Fang³

et al. 2014

Genet. Mol. Res.

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ABSTRACT. This study explored the clinical significance of silencer of death domain (SODD) expression in childhood acute lymphoblastic leukemia (ALL) and its influence on chemotherapy as well as the effect of SODD expression on apoptosis of leukemic cells. The expression of SODD proteins in different ALL groups was determined by immunocytochemistry. The SODD RNAi-interfering plasmid was constructed and transferred to Jurkat cells, and the effects of SODD expression on cell proliferation and apoptosis were analyzed using the MTT and FCM methods. The expressions of SODD, Phospho-NF-κB-P65, Bcl-2, and Caspase 3 were detected by Western blot analysis. The expression of SODD proteins was significantly higher in the ALL groups than in the control group (P < 0.05). The positive expression rate of SODD was significantly higher in refractory/relapsed and clinical high-risk groups than in standard-risk, initial treatment, and complete remission groups (P < 0.05). Microtubule-targeting drugs such as vincristine and taxol can notably down-regulate SODD expression during apoptosis, whereas DNR, and Ara-c cannot. The sensitivity of Jurkat cells to chemotherapeutic drugs increased with down-regulated SODD expression induced by SODD-interfering plasmid transfection. The sensitivity of the cells transfected with SODD-cloning genes decreased. SODD expression was high in the ALL children. These findings indicated that SODD over-expression might be correlated with the clinical classification, curative effect, and prognosis of ALL cells. Microtubule-targeting drugs can specifically down-regulate SODD expression in leukemic cells, thereby increasing the sensitivity of leukemic cells to SODD-targeting chemotherapeutics. In contrast, increased SODD expression tends to reduce sensitivity.

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BAG4/SODD Protein Contains a Short BAG Domain

Cited by 54 publications

References 26 publications

Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists

Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists

Drosophila starvin Encodes a Tissue-Specific BAG-Domain Protein Required for Larval Food Uptake

Significance of SODD expression in childhood acute lymphoblastic leukemia and its influence on chemotherapy

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