The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole

Article Abstract:

An adaptor protein called AP-3 complex in yeast was identified in relation to the study of cargo-selective transport by way of an alternative pathway from the golgi body going to the vacuole. Results show that alkaline phosphatase pathway serves as an alternative pathway for delivering AP-3 complex in yeast such as Apl6p, Apl5p, Apm3p and Aps3p from the golgi body to the vacuole. These AP complexes are identified as homologous to the AP complex found in mammalian cells.

Carrier proteins, Transport proteins

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The G-beta-gamma sensitivity of a PI3K is dependent upon a tightly associated adaptor, p101

Article Abstract:

Molecular biological techniques were used to characterize the activity of G-beta-gamma-sensitive PI3K using cultured Sf9 insect cells and U937 mammalian cells as host systems. The findings showed that p120 and p101 which are proteins that comprise PI3Ks bind tightly to each other, both in vivo and in vitro. p101 was observed to amplify the effect of G-beta-gamma on the catalytic activity of the PI3K's p120 component from less than 2-fold to greater than 100-fold.

Analysis, Genetic regulation, Cloning, Cell receptors, Cell culture, Tissue culture, Enzymatic analysis

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The binding of AP-1 clathrin adaptor particles to golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein

Article Abstract:

Studies prove that ADP-ribosylation factor (ARF), which was previously shown to facilitate binding to Golgi membranes by the coatomer of non-clathrin-coated vesicles, is also required for the binding of the AP-1 adaptor protein of clathrin-coated vesicles to Golgi membranes. There is a common mechanistic characteristic that is present in all types of vesicle coats.

Adenosine diphosphate

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