Dynamin 2 and BAR domain protein pacsin 2 cooperatively regulate formation and maturation of podosomes

2021 ◽  
Vol 571 ◽  
pp. 145-151
Author(s):  
Jianzhen Li ◽  
Kenshiro Fujise ◽  
Haymar Wint ◽  
Yosuke Senju ◽  
Shiro Suetsugu ◽  
...  
Keyword(s):  
Bar Domain ◽  
Domain Protein ◽  
Dynamin 2

scholarly journals Dynamin-2 controls phagophore maturation

2018 ◽  
Author(s):  
Alejandro Martorell Riera ◽  
Cinta Iriondo Martinez ◽  
Samuel Itskanov ◽  
Janos Steffen ◽  
Brett Roach ◽  
...  
Keyword(s):  
Rapid Growth ◽  
Bar Domain ◽  
Late Endosomes ◽  
Protein Membrane ◽  
Transient Interactions ◽  
Domain Protein ◽  
Membrane Addition ◽  
Membrane Scission ◽  
Dynamin 2

AbstractAutophagy involves rapid growth of phagophores through membrane addition. Newly added membranes are derived from other organelles through vesicles carrying the Atg9 protein. Membrane is delivered by fusing these vesicles with the phagophores. Atg9 is, nevertheless, not incorporated in autophagosomes. We now show that this protein is retrieved from phagophores by fission utilizing Dynamin-2 (Dnm2) as the membrane scission protein. Blocking Atg9 recycling by interfering with Dnm2 helps retain Atg9 in autophagosomes and degrades this protein by autophagy. Dnm2 colocalizes with the BAR domain protein Endophilin-B1 (EndoB1/Bif-1) when autophagy is induced, consistent with transient interactions during Atg9 retrieval. EndoB1 and Dnm2 also control the downstream fusion of phagophores to late endosomes, thus ensuring the completion of phagophores before proceeding to the next stage in the autophagy process. These data provide novel insights into the roles of membrane scission proteins during autophagy.

scholarly journals FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure and function

2018 ◽  
Vol 218 (1) ◽  
pp. 97-111 ◽  
Author(s):  
Liang Wang ◽  
Ziyi Yan ◽  
Helena Vihinen ◽  
Ove Eriksson ◽  
Weihuan Wang ◽  
...  
Keyword(s):  
Mitochondrial Function ◽  
Molecular Mechanisms ◽  
Membrane Curvature ◽  
Mitochondrial Morphology ◽  
Membrane Remodeling ◽  
Mitochondrial Ultrastructure ◽  
Bar Domain ◽  
Bar Domain Proteins ◽  
Domain Protein

Mitochondrial function is closely linked to its dynamic membrane ultrastructure. The mitochondrial inner membrane (MIM) can form extensive membrane invaginations known as cristae, which contain the respiratory chain and ATP synthase for oxidative phosphorylation. The molecular mechanisms regulating mitochondrial ultrastructure remain poorly understood. The Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of diverse cellular processes related to membrane remodeling and dynamics. Whether BAR domain proteins are involved in sculpting membranes in specific submitochondrial compartments is largely unknown. In this study, we report FAM92A1 as a novel BAR domain protein localizes to the matrix side of the MIM. Loss of FAM92A1 caused a severe disruption to mitochondrial morphology and ultrastructure, impairing organelle bioenergetics. Furthermore, FAM92A1 displayed a membrane-remodeling activity in vitro, inducing a high degree of membrane curvature. Collectively, our findings uncover a role for a BAR domain protein as a critical organizer of the mitochondrial ultrastructure that is indispensable for mitochondrial function.

scholarly journals The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration

2011 ◽  
Vol 124 (14) ◽  
pp. 2375-2388 ◽  
Author(s):  
B.-J. de Kreuk ◽  
M. Nethe ◽  
M. Fernandez-Borja ◽  
E. C. Anthony ◽  
P. J. Hensbergen ◽  
...  
Keyword(s):  
Cell Spreading ◽  
Bar Domain ◽  
Domain Protein ◽  
And Migration

scholarly journals A BAR-Domain Protein SH3P2, Which Binds to Phosphatidylinositol 3-Phosphate and ATG8, Regulates Autophagosome Formation in Arabidopsis

2013 ◽  
Vol 25 (11) ◽  
pp. 4596-4615 ◽  
Author(s):  
X. Zhuang ◽  
H. Wang ◽  
S. K. Lam ◽  
C. Gao ◽  
X. Wang ◽  
...  
Keyword(s):  
Autophagosome Formation ◽  
Bar Domain ◽  
Domain Protein ◽  
Phosphatidylinositol 3

P.776 Targeting of an F-BAR domain protein to the synaptic periactive zone ensures uniform size of synaptic vesicles

2020 ◽  
Vol 40 ◽  
pp. S440-S441
Author(s):  
O. Shupliakov ◽  
N. Akkuratova ◽  
O. Korenkova ◽  
K. Onohin ◽  
E. Sopova ◽  
...  
Keyword(s):  
Synaptic Vesicles ◽  
Uniform Size ◽  
Bar Domain ◽  
Domain Protein

scholarly journals F-BAR domain protein Syndapin regulates actomyosin dynamics during apical cap remodeling in syncytial Drosophila embryos

2020 ◽  
Vol 133 (10) ◽  
pp. jcs235846
Author(s):  
Aparna Sherlekar ◽  
Gayatri Mundhe ◽  
Prachi Richa ◽  
Bipasha Dey ◽  
Swati Sharma ◽  
...  
Keyword(s):  
Bar Domain ◽  
Domain Protein ◽  
Drosophila Embryos

scholarly journals Self-Assembly of Filopodia-Like Structures on Supported Lipid Bilayers

Science ◽  
2010 ◽  
Vol 329 (5997) ◽  
pp. 1341-1345 ◽  
Author(s):  
Kwonmoo Lee ◽  
Jennifer L. Gallop ◽  
Komal Rambani ◽  
Marc W. Kirschner
Keyword(s):  
Lipid Bilayers ◽  
Self Assembly ◽  
Membrane Microdomains ◽  
Supported Lipid Bilayers ◽  
Actin Bundles ◽  
Bar Domain ◽  
Egg Extracts ◽  
Domain Protein

Filopodia are finger-like protrusive structures, containing actin bundles. By incubating frog egg extracts with supported lipid bilayers containing phosphatidylinositol 4,5 bisphosphate, we have reconstituted the assembly of filopodia-like structures (FLSs). The actin assembles into parallel bundles, and known filopodial components localize to the tip and shaft. The filopodia tip complexes self-organize—they are not templated by preexisting membrane microdomains. The F-BAR domain protein toca-1 recruits N-WASP, followed by the Arp2/3 complex and actin. Elongation proteins, Diaphanous-related formin, VASP, and fascin are recruited subsequently. Although the Arp2/3 complex is required for FLS initiation, it is not essential for elongation, which involves formins. We propose that filopodia form via clustering of Arp2/3 complex activators, self-assembly of filopodial tip complexes on the membrane, and outgrowth of actin bundles.

scholarly journals Muscle-specific Cavin4 interacts with Bin1 to promote T-tubule formation and stability in developing skeletal muscle

2021 ◽  
Author(s):  
Harriet P. Lo ◽  
Ye-Wheen Lim ◽  
Zherui Xiong ◽  
Nick Martel ◽  
Charles Ferguson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Mechanical Stimulation ◽  
Specific Component ◽  
Tubule Formation ◽  
Bar Domain ◽  
T Tubules ◽  
Domain Protein ◽  
And Function

SummaryThe cavin proteins are essential for caveola biogenesis and function. Here, we identify a role for the muscle-specific component, Cavin4, in skeletal muscle T-tubule development by analyzing two vertebrate systems: mouse and zebrafish. In both models Cavin4 localized to T-tubules and loss of Cavin4 resulted in aberrant T-tubule maturation. In zebrafish, which possess duplicated cavin4 paralogs, Cavin4b was shown to directly interact with the T-tubule-associated BAR domain protein, Bin1. Loss of both Cavin4a and Cavin4b caused aberrant accumulation of interconnected caveolae within the T-tubules, a fragmented T-tubule network enriched in Caveolin-3, and an impaired Ca2+ response upon mechanical stimulation. We propose a role for Cavin4 in remodeling the T-tubule membrane early in development by recycling caveolar components from the T-tubule to the sarcolemma. This generates a stable T-tubule domain lacking caveolae that is essential for T-tubule function.

Sign in / Sign up

Export Citation Format

Share Document