Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

Article Abstract:

Researchers have analyzed retrograde protein transport for endoplasmic reticulum (ER) degradation using yeast strains carrying mutant alleles of translocon components. Mutated yeast carboxypeptidase yscY (CPY) was used as a substrate for ER degradation. It was possible to provide functional support for the view that components of the translocon play a role in retrograde protein translocation. It is likely that the translocon subunit Sec61p, and probably also Sec63p and the ER lumenal chaperone BiP (Kar2p), are components of a universally acting subcomplex controlling retrograde transport out of the ER.

Physiological aspects, Endoplasmic reticulum

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AMPA receptor-mediated regulation of a Gi-protein in cortical neurons

Article Abstract:

Intracellular signals that are independent of Ca2+ and Na+ can be generated in rat cortical neurons by the binding of the agonist alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) to its receptor. Changes in a guanine-nucleotide-binding protein were brought about by AMPA when intracellular Ca2+ and Na+ were not present, but not by N-methyl-D-aspartate (NMDA). The AMPA receptor may be similar to the nicotinic acetylcholine receptor, which also seems to be able to activate second messenger systems.

Neural transmission, Neural transmission regulation

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Slow and fast dietary proteins

Article Abstract:

Boirie and colleagues have applied the concept of slow and fast proteins by analogy with dietary carbohydrates, according to the speed at which proteins are digested and amino acids are absorbed. They have concluded that slow and fast proteins can differentially control whole-body protein deposition following a meal.

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