Ramanujan S. Hegde

The paper curates and analyzes topologic determinants of human membrane proteins, identifying key features of transmembrane domains and their implications for function and evolution.

The paper presents the cryo-EM structure of the UBR4 complex, revealing its architecture and mechanism for substrate binding and ubiquitin chain extension in protein quality control.

The paper shows that the mitochondrial targeting signal (MTS) regulates chaperone dynamics on mitochondrial precursors to buffer degradation and maintain import competence during stress.

The paper identifies the UBR4-KCMF1 ubiquitin ligase complex as a convergence point for quality control pathways that degrade orphan subunits, highlighting its role in protein homeostasis and cancer vulnerability.

The paper shows soluble β-tubulins sequester TTC5 to regulate tubulin mRNA decay, with loss of sequestration leading to reduced mRNA levels and chromosome segregation defects.

This paper identifies NACHO as an ER-resident protein that facilitates the assembly of pentameric ligand-gated ion channels by interacting with subunit interfaces.

The paper identifies how TTC5 recruits SCAPER to initiate tubulin mRNA degradation via interaction with the CCR4-NOT complex, linking ribosome-associated mRNA decay to microtubule regulation.

The paper proposes that SecY and YidC originated from a common ancestor through duplication and divergence, unifying their evolutionary origins.