Moving protein heads for breakdown

Article Abstract:

Cell transit requires a delicate balance between positive and negative regulatory factors, and alterations to the balance can lead to abnormal cell proliferation. Proteins can be inactivated by selective protein turnover and are often flagged for destruction with the addition of a phosphate group. Tomoda and colleagues have reported that for the protein p27Kip1, proteasome-mediated degradation needs both phosphorylation and export from the nucleus. They chose proteins that interact with p27Kip1, and a mouse protein Jab1 interacted with P27Kip1. Rising levels of Jab1 led to further breakdown of p27Kip1 and the blocking effect of p27Kip1 was overcome, indicating the Jab1 controls the activity of p27Kip1.

Observations, Cell cycle, Phosphorylation

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Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade

Article Abstract:

The byproduct, ubiquitin thioester on E6-AP, of E6-AP-dependent ubiquitination is an E3 enzyme associated with the human papillomavirus E6-stimulated ubiquitination of p53. The ubiquitin thioester is initially transferred from E1 to E2, from E2 to E6-AP and then to a substrate from E6-AP. The ubiquitin thioester complexes reveal that the enzymes involved in ubiquitin formation possess a definite enzymatic activity and are not docking proteins.

Esters, Ubiquitin

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Proteolytic relay comes to an end

Article Abstract:

Issues are presented concerning the targeting of proteins within the cell by cellular protein-degrading machinery. The signals displayed by target proteins to attract protein-degrading machinery are discussed.

Physiological aspects, Cells (Biology), Physiological regulation, Cells, Biological control systems

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