basic FUNCTION
| acting as a positive cochaperone of Hsp70 |
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critical role of DNAJA1 in spermiogenesis, suggesting that likely DNAJA1 and DNAJA2 are not functionally equivalent |
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factor in the protection against prion diseases (Beck 2006) |
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modulates G protein signaling and further suggest that chaperoning G proteins is an emerging theme of the J protein network (Rosales-Hernandez 2009) |
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key modulator of KCNH2 degradation (Walker 2010) |
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with DNAJA1, cause a decrease in the amount of KCNH2 complexed with Hsc70, indicating a preferential degradation of the complex (Walker 2010) |
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role for the DJA proteins in regulating degradation suggesting that they act at a critical point in secretory pathway quality control (Walker 2010) |
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although functions of DNAJA2 and DNAJA1 independent of HSPA8 are possible, it is generally thought that their main roles are as co-chaperones of HSPA8 |
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DNAJA2 is an unexpected, but potent, inhibitor of MAPT aggregation |
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DNAJA2 and DNAJA1 were both important for CFTR folding, however overexpressing DNAJA2 but not DNAJA1 enhanced CFTR degradation at the endoplasmic reticulum by HSPA4/HSPA8 and the E3 ubiquitin ligase STUB1 |