[HTML][HTML] Cdc48: a swiss army knife of cell biology
Cdc48 (also called VCP and p97) is an abundant protein that plays essential regulatory
functions in a broad array of cellular processes. Working with various cofactors, Cdc48 …
functions in a broad array of cellular processes. Working with various cofactors, Cdc48 …
[HTML][HTML] SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle
C Figueroa-Romero, JA Iñiguez-Lluhí, J Stadler… - The FASEB …, 2009 - ncbi.nlm.nih.gov
Abstract Dynamin-related protein (Drp) 1 is a key regulator of mitochondrial fission and is
composed of GTP-binding, Middle, insert B, and C-terminal GTPase effector (GED) domains …
composed of GTP-binding, Middle, insert B, and C-terminal GTPase effector (GED) domains …
[PDF][PDF] The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes
R Hartmann-Petersen, M Wallace, K Hofmann, G Koch… - Current biology, 2004 - cell.com
Valosin-containing protein, VCP/p97 or Cdc48, is a eukaryotic ATPase involved in
membrane fusion, protein transport, and protein degradation. We describe two proteins …
membrane fusion, protein transport, and protein degradation. We describe two proteins …
Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51–Rad52 interaction
S Bergink, T Ammon, M Kern, L Schermelleh… - Nature cell …, 2013 - nature.com
Cdc48 (also known as p97), a conserved chaperone-like ATPase, plays a strategic role in
the ubiquitin system,,. Empowered by ATP-driven conformational changes, Cdc48 acts as a …
the ubiquitin system,,. Empowered by ATP-driven conformational changes, Cdc48 acts as a …
Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling
W Li, MH Bengtson, A Ulbrich, A Matsuda, VA Reddy… - PloS one, 2008 - journals.plos.org
Specificity of protein ubiquitylation is conferred by E3 ubiquitin (Ub) ligases. We have
annotated∼ 617 putative E3s and substrate-recognition subunits of E3 complexes encoded …
annotated∼ 617 putative E3s and substrate-recognition subunits of E3 complexes encoded …
Mitochondrial fusion and fission in cell life and death
B Westermann - Nature reviews Molecular cell biology, 2010 - nature.com
Mitochondria are dynamic organelles that constantly fuse and divide. These processes
(collectively termed mitochondrial dynamics) are important for mitochondrial inheritance and …
(collectively termed mitochondrial dynamics) are important for mitochondrial inheritance and …
The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
Mitochondrial fusion and structure depend on the dynamin-like GTPase OPA1, whose
activity is regulated by proteolytic processing. Constitutive OPA1 cleavage by YME1L and …
activity is regulated by proteolytic processing. Constitutive OPA1 cleavage by YME1L and …
Human Fis1 regulates mitochondrial dynamics through inhibition of the fusion machinery
Mitochondrial dynamics is important for life. At center stage for mitochondrial dynamics, the
balance between mitochondrial fission and fusion is a set of dynamin‐related GTP ases that …
balance between mitochondrial fission and fusion is a set of dynamin‐related GTP ases that …
[HTML][HTML] New insights into mitochondrial fusion
Y Zhang, DC Chan - FEBS letters, 2007 - Elsevier
Fusion controls mitochondrial morphology and is important for normal mitochondrial
function, including roles in respiration, development, and apoptosis. Key components of the …
function, including roles in respiration, development, and apoptosis. Key components of the …
Redox modifications of proteins of the mitochondrial fusion and fission machinery
Mitochondrial fusion and fission tailors the mitochondrial shape to changes in cellular
homeostasis. Players of this process are the mitofusins, which regulate fusion of the outer …
homeostasis. Players of this process are the mitofusins, which regulate fusion of the outer …