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Filamins but not Janus kinases are substrates of the ASB2? cullin-ring E3 ubiquitin ligase in hematopoietic cells.


ABSTRACT: The ASB2? protein is the specificity subunit of an E3 ubiquitin ligase complex involved in hematopoietic differentiation and is proposed to exert its effects by regulating the turnover of specific proteins. Three ASB2? substrates have been described so far: the actin-binding protein filamins, the Mixed Lineage Leukemia protein, and the Janus kinases 2 and 3. To determine the degradation of which substrate drives ASB2? biological effects is crucial for the understanding of ASB2? functions in hematopoiesis. Here, we show that neither endogenous nor exogenously expressed ASB2? induces degradation of JAK proteins in hematopoietic cells. Furthermore, we performed molecular modeling to generate the first structural model of an E3 ubiquitin ligase complex of an ASB protein bound to one of its substrates.

SUBMITTER: Lamsoul I 

PROVIDER: S-EPMC3423375 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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Filamins but not Janus kinases are substrates of the ASB2α cullin-ring E3 ubiquitin ligase in hematopoietic cells.

Lamsoul Isabelle I   Erard Monique M   van der Ven Peter F M PF   Lutz Pierre G PG  

PloS one 20120820 8


The ASB2α protein is the specificity subunit of an E3 ubiquitin ligase complex involved in hematopoietic differentiation and is proposed to exert its effects by regulating the turnover of specific proteins. Three ASB2α substrates have been described so far: the actin-binding protein filamins, the Mixed Lineage Leukemia protein, and the Janus kinases 2 and 3. To determine the degradation of which substrate drives ASB2α biological effects is crucial for the understanding of ASB2α functions in hema  ...[more]

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