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The proliferating cell nuclear antigen (PCNA) processivity factor provides a central regulatory platform during DNA replication and associated processes, including DNA damage repair. The interaction of PCNA with many cellular proteins is key to this function and is subject to tight, multilayered control.
As well as degrading and recycling cellular waste, lysosomes are involved in secretion, plasma membrane repair, signalling and energy metabolism. The identification of transcription factor EB (TFEB) as a central regulator of lysosomal biogenesis and autophagy provides insight into how lysosomes adapt to environmental cues, and targeting TFEB may be a promising therapeutic strategy for modulating lysosomal function in disease.
Recent work on the structure and function of the RB protein revealed its multifunctionality in cancer and during normal physiology. Remarkably, additional tumour-suppressor functions have come to light, including new roles in cell cycle regulation, maintenance of genome stability and apoptosis.
The transmembrane protein Crumbs is known to maintain epithelial polarity and regulate Notch and Hippo signalling via its short intracellular domain. Recent evidence now suggests that its extracellular domain has a conserved and fundamental role in mediating homophilic Crumbs–Crumbs interactions at cell–cell junctions.
The distribution of partitioning defective (PAR) proteins into two domains on the membrane is a hallmark of cell polarity. Domain boundaries are set by mechanical, biochemical and biophysical signals, and the resulting PAR domains define areas of cytosol specialization. Physical studies are now contributing to the understanding of the mechanisms underlying polarity establishment by PAR proteins.