How proteins penetrate peroxisomes

Article Abstract:

The movement of proteins into the peroxisomal lumen involves the recognition of a peroxisomal targeting signal (PTS) by its cognate receptors. The receptors target the proteins to the translocation pathway. Proteins without a PTS associate with the PTS-containing proteins to penetrate the peroxisome. The PTS1 receptors of yeast and humans are structurally similar. In human peroxisomal diseases, the translocation of proteins is defective. Peroxisomes are able to translocate oligomeric proteins unlike the mitochondria and chloroplast.

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Crystal structure of the tyrosine phosphatase SHP-2

Article Abstract:

Research was conducted to study the crystal structure of the SHP-2 tyrosine phosphatase determined at 2.0 angstrom resolution. Recombinant human SHP-2 was determined in Escherichia coli and isolated by sequential column chromatography. Results indicated that SHP-2's catalytic activity was regulated by two domains. They also showed the disruption of active sites and the blocking of ligand surfaces of the SH3 and SH2 tyrosine phosphatase domains.

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Regulatio of Golgi structure through heterotrimeric G proteins

Article Abstract:

It has been shown that ilimaquinone (IQ), a marine sponge metabolite, can cause vesiculation of the Golgi stacks. It has also been shown that the process does not require ARF and coatomers. IQ-mediated Golgi vesiculation was found to be inhibited by Galphas-GDP and Galpha13-GDP, and that the free Betagamma triggers Golgi vesiculation.

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