Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis (Q24306444)

ubiquitin-protein transferase activity

GOA release 2020-03-11

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GOA release 2020-03-11

author name string

Qing Zhong

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Wenhua Gao

2

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Fenghe Du

3

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Xiaodong Wang

MCL-1, a member of the BLC-2 family, is induced rapidly in response to signals for cell differentiation or death, but not to signals for cell proliferation

4

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publication date

1 July 2005

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language of work or name

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121

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issue

7

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page(s)

1085-95

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cites work

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The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation

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The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway

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SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27

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Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade

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Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics

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Development and maintenance of B and T lymphocytes requires antiapoptotic MCL-1.

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Proteins containing the UBA domain are able to bind to multi-ubiquitin chains

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Cleavage of Mcl-1 by caspases impaired its ability to counteract Bim-induced apoptosis.

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Survival factor-induced extracellular signal-regulated kinase phosphorylates BIM, inhibiting its association with BAX and proapoptotic activity.

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A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase

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Granulocyte macrophage colony-stimulating factor signaling and proteasome inhibition delay neutrophil apoptosis by increasing the stability of Mcl-1.

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Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation

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DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells

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