A highly conserved BECN1 domain located between previously characterized BH3 and coiled-coil domains is delineated and its structure and role in autophagy is elucidated.
The integrative structural model of full-length HsNHE6 provides a framework for understanding HsNHE6-mediated ion exchange and its disruption in Christianson syndrome and shows a kinetic preference for K+ over Na+ transport.
L. P. Feilen, Lara Sach, Emil E. Tranchant et al.· Nature Communications· 1 citation
This work establishes that multisite phosphorylation of the SPT5 CTR1 domain modulates a heterogeneous interaction landscape shaped by sequence context, and emphasizes the nontrivial difference between serine and threonine phosphorylation as a mechanism to regulate disordered protein structure–function relationships.
Rong Hu, E. Usher, Olivia A Fraser et al.· Journal of Physical Chemistr...· 0 citations
The Keap1-Nrf2 system plays a central role in cellular defense against oxidative stress. Structural information on full-length Keap1 is essential for understanding the molecular basis of this regulation. However, its overall architecture has remained elusive due to pronounced conformational flexibility. In this study,...
Ritsumi Saito, Takeshi Kawabata, S. Yamashita et al.· Redox Biology· 0 citations
A phosphorylation-triggered order-to-disorder transition that relieves FOXM1 autoinhibition and highlight Ser715 as a key structural and energetic switch is supported and provided a dynamic molecular framework for targeting FOXM1 activation via its regulatory fold.
Sara AlRawashdeh, Raghd Obidat, Aylin del Moral-Morales et al.· Journal of Chemical Informat...· 1 citation
Macroautophagy is a conserved catabolic process that facilitates the degradation of cellular material by capturing it in double membrane vesicles termed autophagosomes. In Saccharomyces cerevisiae, selective macroautophagy is initiated by the scaffolding protein Atg11. Atg11 recruits the transmembrane protein Atg9, whi...
Sarah I Najera, Devika Andhare, Anna E. Hill et al.· bioRxiv· 0 citations
It is shown that DM3 reversibly assembles into higher-order filaments in a salt-sensitive manner, which reveals how structural plasticity in protein assemblies enables a single protein to coordinate multiple stress-response functions, highlighting a general mechanism for regulating protein activity in plants.
Nayun Kim, Wei-Lin Wan, Yi-Yun Tan et al.· bioRxiv· 0 citations
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