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Phosphorylation cycles on vesicles

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Cargo recruitment is mediated by the μ1 subunit of AP-1... The authors demonstrate that μ1 is phosphorylated on the membrane and dephosphorylated in the cytosol... Phosphorylation induced a conformational change in μ1 that increased its affinity for cargo ligands... In combination, PP2A and Hsc-70 released both AP-1 and AP-2 from vesicles in vitro, suggesting that dephosphorylation is a common uncoating mechanism... In addition to μ1, PP2A had another target in the AP-1 complex... But unlike μ1, this second substrate, the β1 subunit, was dephosphorylated on the Golgi rather than on vesicles... As β1 phosphorylation impairs its ability to interact with clathrin, PP2A activity is necessary for CCV formation... The opposing preference for substrates based on location (Golgi-associated PP2A preferred β1, whereas vesicle-associated PP2A favored μ1) thus restricts the activity of each subunit to the desired location. ▪

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Dephosphorylation of μ1 releases it from cargo and lets AP-1 off vesicles.
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uro1: Dephosphorylation of μ1 releases it from cargo and lets AP-1 off vesicles.


Phosphorylation cycles on vesicles
Dephosphorylation of μ1 releases it from cargo and lets AP-1 off vesicles.
© Copyright Policy
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC2255596&req=5

uro1: Dephosphorylation of μ1 releases it from cargo and lets AP-1 off vesicles.

View Article: PubMed Central

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

Cargo recruitment is mediated by the μ1 subunit of AP-1... The authors demonstrate that μ1 is phosphorylated on the membrane and dephosphorylated in the cytosol... Phosphorylation induced a conformational change in μ1 that increased its affinity for cargo ligands... In combination, PP2A and Hsc-70 released both AP-1 and AP-2 from vesicles in vitro, suggesting that dephosphorylation is a common uncoating mechanism... In addition to μ1, PP2A had another target in the AP-1 complex... But unlike μ1, this second substrate, the β1 subunit, was dephosphorylated on the Golgi rather than on vesicles... As β1 phosphorylation impairs its ability to interact with clathrin, PP2A activity is necessary for CCV formation... The opposing preference for substrates based on location (Golgi-associated PP2A preferred β1, whereas vesicle-associated PP2A favored μ1) thus restricts the activity of each subunit to the desired location. ▪

No MeSH data available.


Related in: MedlinePlus