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

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 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 ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ

2019 ◽  
Vol 218 (5) ◽  
pp. 1634-1652 ◽  
Author(s):  
Delphine Judith ◽  
Harold B.J. Jefferies ◽  
Stefan Boeing ◽  
David Frith ◽  
Ambrosius P. Snijders ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Amino Acid ◽  
Membrane Protein ◽  
Initiation Site ◽  
Amino Acid Starvation ◽  
Autophagosome Formation ◽  
Metabolizing Enzymes ◽  
Bar Domain ◽  
Golgi Membranes ◽  
Phosphatidylinositol 4

ATG9A is a multispanning membrane protein essential for autophagy. Normally resident in Golgi membranes and endosomes, during amino acid starvation, ATG9A traffics to sites of autophagosome formation. ATG9A is not incorporated into autophagosomes but is proposed to supply so-far-unidentified proteins and lipids to the autophagosome. To address this function of ATG9A, a quantitative analysis of ATG9A-positive compartments immunoisolated from amino acid–starved cells was performed. These ATG9A vesicles are depleted of Golgi proteins and enriched in BAR-domain containing proteins, Arfaptins, and phosphoinositide-metabolizing enzymes. Arfaptin2 regulates the starvation-dependent distribution of ATG9A vesicles, and these ATG9A vesicles deliver the PI4-kinase, PI4KIIIβ, to the autophagosome initiation site. PI4KIIIβ interacts with ATG9A and ATG13 to control PI4P production at the initiation membrane site and the autophagic response. PI4KIIIβ and PI4P likely function by recruiting the ULK1/2 initiation kinase complex subunit ATG13 to nascent autophagosomes.

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 Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum

2008 ◽  
Vol 182 (4) ◽  
pp. 685-701 ◽  
Author(s):  
Elizabeth L. Axe ◽  
Simon A. Walker ◽  
Maria Manifava ◽  
Priya Chandra ◽  
H. Llewelyn Roderick ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Dynamic Equilibrium ◽  
Membrane Vesicles ◽  
Amino Acid Starvation ◽  
Autophagosome Formation ◽  
Double Membrane ◽  
Dynamic Relationship ◽  
Golgi Membranes ◽  
Membrane Compartments ◽  
Phosphatidylinositol 3

Autophagy is the engulfment of cytosol and organelles by double-membrane vesicles termed autophagosomes. Autophagosome formation is known to require phosphatidylinositol 3-phosphate (PI(3)P) and occurs near the endoplasmic reticulum (ER), but the exact mechanisms are unknown. We show that double FYVE domain–containing protein 1, a PI(3)P-binding protein with unusual localization on ER and Golgi membranes, translocates in response to amino acid starvation to a punctate compartment partially colocalized with autophagosomal proteins. Translocation is dependent on Vps34 and beclin function. Other PI(3)P-binding probes targeted to the ER show the same starvation-induced translocation that is dependent on PI(3)P formation and recognition. Live imaging experiments show that this punctate compartment forms near Vps34-containing vesicles, is in dynamic equilibrium with the ER, and provides a membrane platform for accumulation of autophagosomal proteins, expansion of autophagosomal membranes, and emergence of fully formed autophagosomes. This PI(3)P-enriched compartment may be involved in autophagosome biogenesis. Its dynamic relationship with the ER is consistent with the idea that the ER may provide important components for autophagosome formation.

scholarly journals Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L

2010 ◽  
Vol 190 (4) ◽  
pp. 511-521 ◽  
Author(s):  
Kohichi Matsunaga ◽  
Eiji Morita ◽  
Tatsuya Saitoh ◽  
Shizuo Akira ◽  
Nicholas T. Ktistakis ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mammalian Cells ◽  
Embryonic Stem ◽  
Pi3 Kinase ◽  
Class Iii ◽  
Autophagosome Formation ◽  
Membranous Structure ◽  
Er Targeting ◽  
Endoplasmic Reticulum Targeting ◽  
Phosphatidylinositol 3

Autophagy is a catabolic process that allows cells to digest their cytoplasmic constituents via autophagosome formation and lysosomal degradation. Recently, an autophagy-specific phosphatidylinositol 3-kinase (PI3-kinase) complex, consisting of hVps34, hVps15, Beclin-1, and Atg14L, has been identified in mammalian cells. Atg14L is specific to this autophagy complex and localizes to the endoplasmic reticulum (ER). Knockdown of Atg14L leads to the disappearance of the DFCP1-positive omegasome, which is a membranous structure closely associated with both the autophagosome and the ER. A point mutation in Atg14L resulting in defective ER localization was also defective in the induction of autophagy. The addition of the ER-targeting motif of DFCP1 to this mutant fully complemented the autophagic defect in Atg14L knockout embryonic stem cells. Thus, Atg14L recruits a subset of class III PI3-kinase to the ER, where otherwise phosphatidylinositol 3-phosphate (PI3P) is essentially absent. The Atg14L-dependent appearance of PI3P in the ER makes this organelle the platform for autophagosome formation.

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
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