FBXL5 interacts with p150Glued and regulates its ubiquitination (Q24307388)

GOA release 2020-03-11

protein ubiquitination

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Ning Zhang

1

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Jing Liu

2

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Xia Ding

3

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Felix Aikhionbare

4

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Changjiang Jin

5

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Xuebiao Yao

Biochemical and Biophysical Research Communications

6

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language of work or name

English

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publication date

20 July 2007

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published in

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volume

359

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issue

1

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page(s)

34-9

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cites work

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A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules.

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Sequence analysis of the complete cDNA and encoded polypeptide for the Glued gene of Drosophila melanogaster

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The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)

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Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin

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Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

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Apoptotic cleavage of cytoplasmic dynein intermediate chain and p150(Glued) stops dynein-dependent membrane motility.

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