HSP70-binding protein HSPBP1 regulates chaperone expression at a posttranslational level and is essential for spermatogenesis

Rogon, Christian; Ulbricht, Anna; Hesse, Michael; Alberti, Simon; Vijayaraj, Preethi; Best, Diana; Adams, Ian R.; Magin, Thomas M.; Fleischmann, Bernd K.; Höhfeld, Jörg

doi:10.1091/mbc.e14-02-0742

Cited by 27 publications

(19 citation statements)

References 71 publications

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“…HSPA2 expression in testis can be regulated at posttranslational level by proteins such as the following: the multifunctional Bat3 (HLA-B-associated transcript 3, also known as BAG6) chaperone belonging to BCL2-associated athanogene (BAG) domain protein family (Sasaki et al 2008 ; Kawahara et al 2013 ); HSPA binding protein HSPBP1, a nucleotide exchange factor of HSPA proteins and inhibitor of protein degradation mediated by the carboxy terminus of HSP70 interacting protein CHIP (Rogon et al 2014 ); and eukaryotic translation initiation factor 4 gamma 3 (Eif4g3, Sun et al 2010 ).…”

Section: Regulation Of the Expression Of The Hspa2mentioning

confidence: 99%

“…Bat3 and the co-chaperone HSPBP1 were shown to bind to HSPA2 and prevent its ubiquitination and proteasomal degradation in the testis (Sasaki et al 2008 ; Rogon et al 2014 ). Deficiency of Bat3, or HSPBP1, in knockout (KO) mice leads to male infertility caused by impaired spermatogenesis with morphological features similar to those observed in HSPA2 null mice.…”

Section: Regulation Of the Expression Of The Hspa2mentioning

confidence: 99%

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Expression, function, and regulation of the testis-enriched heat shock HSPA2 gene in rodents and humans

Ścieglińska

Krawczyk

2015

Cell Stress and Chaperones

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The HSPA2 gene is a poorly characterized member of the HSPA (HSP70) family. HSPA2 was originally described as testis-specific and expressed at the highest level in pachytene spermatocytes of rodents, the expression of which is not induced by heat shock. HSPA2 is crucial for male fertility. However, recent advances have shown that HSPA2 is expressed in various tumors and in certain types of somatic tissues. In this review, we summarize the current knowledge on the HSPA2 expression pattern, including information on transcriptional, translational, posttranslational, and epigenetic mechanisms which regulate HSPA2 expression. We also present and discuss the current views concerning the functions of the HSPA2 protein in spermatogenetic, somatic, and cancer cells. The knowledge of the properties of HSPA2, although limited, shows this protein as a unique member of the HSPA family. However, understanding whether this protein could become a relevant cancer biomarker or a therapeutically applicable target requires extensive further studies.

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Section: Regulation Of the Expression Of The Hspa2mentioning

confidence: 99%

Section: Regulation Of the Expression Of The Hspa2mentioning

confidence: 99%

Expression, function, and regulation of the testis-enriched heat shock HSPA2 gene in rodents and humans

Ścieglińska

Krawczyk

2015

Cell Stress and Chaperones

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“…Their functions under the physiologic conditions of meiosis have been extensively investigated. Gene knockout experiments have shown that testis-enriched Hsp70-2 (17)(18)(19), the Hsp105/110 family protein HSPA4 (20), and Hsp70-2 binding-protein HspBP1 (21) contribute to proper meiotic progression in the development of sperm cells. Among these, Hsp70-2 is essential for cyclin-dependent kinase (Cdk) 1 kinase activity in spermatocytes through its interaction with Cdk1 (19).…”

mentioning

confidence: 99%

Heat shock‐induced mitotic arrest requires heat shock protein 105 for the activation of spindle assembly checkpoint

et al. 2018

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Heat shock causes proteotoxic stress that induces various cellular responses, including delayed mitotic progression and the generation of an aberrant number of chromosomes. In this study, heat shock delayed the onset of anaphase by increasing the number of misoriented cells, accompanied by the kinetochore localization of budding uninhibited by benzimidazole–related (BubR)1 in a monopolar spindle (Mps)l‐dependent manner. The mitotic delay was canceled by knockdown of mitotic arrest defect (Mad)2. Knockdown of heat shock protein (Hsp)105 partially abrogated the mitotic delay with the loss of the kinetochore localization of BubR1 under heat shock conditions and accelerated mitotic progression under nonstressed conditions. Consistent with this result, Hsp105 knockdown increased the number of anaphase cells with lagging chromosomes, through mitotic slippage, and decreased taxol sensitivity more than Mad2 knockdown. Hsp105 was coprecipitated with cell division cycle (Cdc)20 in an Mps1‐dependent manner; however, its knockdown did not affect coprecipitation of Mad2 and BubR1 with Cdc20. We propose that heat shock delays the onset of anaphase via the activation of the spindle assembly checkpoint (SAC). Hsp105 prevents abnormal cell division by contributing to SAC activation under heat shock and nonstressed conditions by interacting with Cdc20 but not affecting formation of the mitotic checkpoint complex.—Kakihana, A., Oto, Y., Saito, Y., Nakayama, Y. Heat shock‐induced mitotic arrest requires heat shock protein 105 for the activation of spindle assembly checkpoint. FASEB J. 33, 3936–3953 (2019). http://www.fasebj.org

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“…We speculate that these proteins may play vital roles in the maturation and cell proliferation of buffalo testicular seminiferous tubules. For example, HSPA2 has been validated to be involved in spermatogenesis and male fertility in previous studies (Govin et al., ; Huang et al., ; Rogon et al., ). The Sertoli cell VIM protein filaments play an important role in the maintenance of spermatogenesis and the vimentin can be reorganized after the germ cells repopulate and spermatogenesis is restored (Kuznetsov, Froberg, Henlon, Reinke, & Fennelly, ).…”

Section: Discussionmentioning

confidence: 97%

Comparative proteomic analysis of different developmental stages of swamp buffalo testicular seminiferous tubules

Zhang

et al. 2017

Reprod Domestic Animals

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With ageing, many protein components change markedly during mammalian spermatogenesis. Most of these proteins have yet to be characterized and verified. Here, we have employed two-dimensional electrophoresis coupled to tandem mass spectrometry to explore the different proteins from pre-pubertal, pubertal and post-pubertal swamp buffalo testicular seminiferous tubules. The results showed that 25 protein spots were differentially expressed among developmental stages, and 13 of them were successfully identified by mass spectrometry. Of which four proteins were up-regulated and three proteins were down-regulated with age, and the remaining six proteins were fluctuated among developmental stages. Bioinformatics analysis indicates that these proteins were probably related to cellular developmental process (53.8%), cell differentiation (53.8%), spermatogenesis (15.4%), apoptotic process and cell death (30.8%). Expression profiles of calumenin (CALU) and galectin-1 (LGALS1) were further verified via Western blotting. In summary, the results help to develop an understanding of molecular mechanisms associated with buffalo spermatogenesis.

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HSP70-binding protein HSPBP1 regulates chaperone expression at a posttranslational level and is essential for spermatogenesis

Cited by 27 publications

References 71 publications

Expression, function, and regulation of the testis-enriched heat shock HSPA2 gene in rodents and humans

Expression, function, and regulation of the testis-enriched heat shock HSPA2 gene in rodents and humans

Heat shock‐induced mitotic arrest requires heat shock protein 105 for the activation of spindle assembly checkpoint

Comparative proteomic analysis of different developmental stages of swamp buffalo testicular seminiferous tubules

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