We provide direct evidence that Bin/Amphiphysin/Rvs (BAR) family members bend the steady state membrane architecture of organelles in intact cells. In response to inducible BAR molecular actuators, organelles exhibit distinct changes to the orientation and degree of their membrane curvature. This rapidly inducible system may offer a mechanism by which to better understand the structure-function relationship of intracellular organelles.
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http://dx.doi.org/10.1038/srep04693 | DOI Listing |
Life Sci Alliance
February 2025
Molecular and Cellular Biology Graduate Program, Stony Brook University, Stony Brook, NY, USA
Bin/Amphiphysin/Rvs (BAR) domains are highly conserved domains found in all eukaryotes. BAR domain proteins form crescent-shaped dimers that sense and sculpt curved lipid membranes and play key roles in various cellular processes. However, their functions in mammalian development are poorly understood.
View Article and Find Full Text PDFJ Biol Chem
October 2024
Université Côte d'Azur, CNRS, INSERM, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France. Electronic address:
Traffic
July 2024
State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
SNX32 is a member of the evolutionarily conserved Phox (PX) homology domain- and Bin/Amphiphysin/Rvs (BAR) domain- containing sorting nexin (SNX-BAR) family of proteins, which play important roles in sorting and membrane trafficking of endosomal cargoes. Although SNX32 shares the highest amino acid sequence homology with SNX6, and has been believed to function redundantly with SNX5 and SNX6 in retrieval of the cation-independent mannose-6-phosphate receptor (CI-MPR) from endosomes to the trans-Golgi network (TGN), its role(s) in intracellular protein trafficking remains largely unexplored. Here, we report that it functions in parallel with SNX1 in mediating epidermal growth factor (EGF)-stimulated postendocytic trafficking of the epidermal growth factor receptor (EGFR).
View Article and Find Full Text PDFNat Commun
July 2024
Mental Health Center and National Chengdu Center for Safety Evaluation of Drugs, State Key Laboratory of Biotherapy, West China Hospital of Sichuan University, Chengdu, 610041, China.
The Bin/Amphiphysin/Rvs (BAR) domain protein FAM92A1 is a multifunctional protein engaged in regulating mitochondrial ultrastructure and ciliogenesis, but its physiological role in the brain remains unclear. Here, we show that FAM92A1 is expressed in neurons starting from embryonic development. FAM92A1 knockout in mice results in altered brain morphology and age-associated cognitive deficits, potentially due to neuronal degeneration and disrupted synaptic plasticity.
View Article and Find Full Text PDFHeliyon
July 2024
Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Indore bypass Road, Bhopal 462 066, Madhya Pradesh, India.
Intracellular membrane tubules play a crucial role in diverse cellular processes, and their regulation is facilitated by Bin-Amphiphysin-Rvs (BAR) domain-containing proteins. This study investigates the roles of ICA69 (dICA69) (an N-BAR protein) and CIP4 (dCIP4) (an F-BAR protein), focusing on their impact on membrane tubule organization. In contrast to the prevailing models of BAR-domain protein function, we observed colocalization of endogenous dICA69 with dCIP4-induced tubules, indicating their potential recruitment for tubule formation and maintenance.
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