Publications by authors named "Kristofer R Gonzalez-DeWhitt"
Article Synopsis
- The voltage-dependent anion channel (VDAC) is a key protein in mitochondria that helps exchange ions and metabolites with the cytosol, and its structure was first defined in 2008.
- The recent study presents a new crystal structure of mouse VDAC-1 at room temperature, revealing differences in its loop regions compared to previous cryogenic images, which may be vital for how VDAC-1 opens and closes.
- The research suggests using electric field-stimulated X-ray crystallography (EF-X) to study the 'closed' state of VDAC-1, aiming to better understand its dynamic gating mechanism and overall role in mitochondrial functions.
The serine/threonine protein phosphatase 1 (PP1) dephosphorylates hundreds of key biological targets by associating with nearly 200 regulatory proteins to form highly specific holoenzymes. However, how these proteins direct PP1 specificity and the ability to predict how these PP1 interacting proteins bind PP1 from sequence alone is still missing. PP1 nuclear targeting subunit (PNUTS) is a PP1 targeting protein that, with PP1, plays a central role in the nucleus, where it regulates chromatin decondensation, RNA processing, and the phosphorylation state of fundamental cell cycle proteins, including the retinoblastoma protein (Rb), p53, and MDM2.
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