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Walczak, C.

Publications and source records attributed to Walczak, C..

2 recordsLinked to original sources

MAFA Phosphorylation Controls Beta-Cell Identity and Sex-Specific Pancreatic Disease Outcomes

Mafa is a critical transcription factor in pancreatic beta-cell biology, orchestrating insulin expression in response to glucose elevations. As a member of the large MAF protein family, MAFAs stability and activity are intricately regulated by GSK3-mediated phosphorylation. To decipher the functional roles of these phosphorylations, we engineered knock-in mice (Mafa4A/+) in which MAFA is rendered non-phosphorylatable. In all Mafa4A/+ animals, MAFA stability was markedly enhanced. Under high-fat diet (HFD) conditions, Mafa4A/+ males rapidly developed glucose intolerance, which was attributed to impaired glucose-stimulated insulin secretion. Bulk RNA sequencing revealed disrupted beta- cell identity, characterized by increased expression of MODY-associated genes and a delta-cell signature, suggesting beta-to-delta cell reprogramming, a hypothesis supported by lineage- tracing experiments. Conversely, Mafa4A/+ females exhibited hypoglycemia and, with age, developed pronounced inflammatory cystic ducts including mucinous cystic neoplasms (MCNs). Strikingly, MAFA protein was also detected in MCN biopsies from female patients, linking our findings to human pathology. Our results unveil a sex-biased impact of GSK3-mediated MAFA phosphorylation. The male phenotype closely parallels the MODY-like diabetes observed in patients with MAFA S64F mutations, implicating defective phosphorylation in disease etiology. The emergence of MCNs in female mice suggests a novel role for MAFA stability or mutations in the pathogenesis of these enigmatic neoplasms, providing a fresh molecular hypothesis with clinical relevance.

cell biology↗

Emerging Roles of Importin alpha/beta and EB1 in Differential Regulation of Kif18B Astral Microtubule Destabilization

Tight regulation of microtubule (MT) dynamics is necessary for proper spindle assembly and chromosome segregation. The MT destabilizing Kinesin-8, Kif18B, controls astral MT dynamics and spindle positioning. Kif18B interacts with importin /{beta} as well as with the plus-tip tracking protein EB1, but how these associations modulate Kif18B is not known. We mapped the key binding sites on Kif18B, made residue-specific mutations, and assessed their impact on Kif18B function. Blocking EB1 interaction disrupted Kif18B MT plus-end accumulation and inhibited its ability to control MT length on monopolar spindles in cells. Blocking importin /{beta} interaction disrupted Kif18B localization without affecting aster size. In vitro, importin /{beta} increased Kif18B MT association by increasing the on-rate and decreasing the off-rate from MTs, which stimulated MT destabilization. In contrast, EB1 promoted MT destabilization without increasing lattice binding in vitro, which suggests that EB1 and importin /{beta} have distinct roles in the regulation of Kif18B-mediated MT destabilization. We propose that importin /{beta}-spatially modulate Kif18B association with MTs to facilitate its MT destabilization activity. Our results suggest that Ran-regulation is important not only to control molecular motor function near chromatin but also provides a spatial control mechanism to modulate MT binding of NLS-containing spindle assembly factors.

cell biology↗