Results 21 to 30 of about 4,209 (249)
Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin. [PDF]
PLoS Genetics, 2005 Ciliates, although single-celled organisms, contain numerous subcellular structures and pathways usually associated with metazoans. How this cell biological complexity relates to the evolution of molecular elements is unclear, because features in these ...
Nels C Elde +4 more
doaj +2 more sources
Dynamin recruitment and membrane scission at the neck of a clathrin-coated pit [PDF]
, 2014 Dynamin, the GTPase required for clathrin-mediated endocytosis, is recruited to clathrin-coated pits in two sequential phases. The first is associated with coated pit maturation; the second, with fission of the membrane neck of a coated pit.
Cocucci, Emanuele +2 more
core +1 more source
American Journal of Medical Genetics Part C: Seminars in Medical Genetics, EarlyView., 2023 Abstract Dynamin 1 is a GTPase protein involved in synaptic vesicle fission, which facilitates the exocytosis of neurotransmitters necessary for normal signaling. Pathogenic variants in the DNM1 gene are associated with intractable epilepsy, often manifested as infantile spasms at onset, developmental delay, and a movement disorder, and are located in ...
Davide Mei +4 more
wiley +1 more source
Phosphorylation of dynamin by ERK2 inhibits the dynamin‐microtubule interaction [PDF]
FEBS Letters, 1996 In the present study we show that purified bovine brain dynamin can be phosphorylated by MAP kinase, ERK2, with a stoichiometry of 1 mol phosphate/mol dynamin. The phosphorylated serine residue is located within the C‐terminal 10 kDa of dynamin. Dynamin I phosphorylated by ERK2 can be specifically dephosphorylated by calcineurin but not by protein ...
Earnest, Svetlana +3 more
openaire +2 more sources
Mitochondrial Membrane Dynamics—Functional Positioning of OPA1
Antioxidants, 2018 The maintenance of mitochondrial energetics requires the proper regulation of mitochondrial morphology, and vice versa. Mitochondrial dynamins control mitochondrial morphology by mediating fission and fusion.
Hakjoo Lee, Yisang Yoon
doaj +1 more source
Dynamin as a Mover and Pincher during Cell Migration and Invasion [PDF]
, 2006 The large GTPase dynamin, long known for its role in endocytosis, has most recently been implicated as a facilitator of cell migration and invasion. Recent observations link dynamin to the cycle of membrane expansion and retraction essential for cell ...
Kruchten, Anne E., McNiven, Mark A.
core +2 more sources
Dynamin 1 is required for memory formation. [PDF]
PLoS ONE, 2014 Dynamin 1-3 isoforms are known to be involved in endocytotic processes occurring during synaptic transmission. No data has directly linked dynamins yet with normal animal behavior.
Mauro Fà +4 more
doaj +1 more source
Domain interactions within Fzo1 oligomers are essential for mitochondrial fusion [PDF]
, 2006 Mitofusins are conserved GTPases essential for the fusion of mitochondria. These mitochondrial outer membrane proteins contain a GTPase domain and two or three regions with hydrophobic heptad repeats, but little is known about how these domains interact ...
Chan, David C., Griffin, Erik E.
core +3 more sources
Dynamin Subunit Interactions Revealed [PDF]
Developmental Cell, 2010 Dynamin family members are large GTPases that assemble into multimeric spirals. These spirals promote membrane fission or fusion, or they inhibit processes such as viral replication. Two new studies by Chappie et al. and Gao et al. in a recent issue of Nature identify interactions between subunits of dynamin spirals, advancing mechanistic understanding
van der Bliek, Alexander M. +1 more
openaire +2 more sources
Smed-dynA-1 is a planarian nervous system specific dynamin 1 homolog required for normal locomotion
Biology Open, 2014 Dynamins are GTPases that are required for separation of vesicles from the plasma membrane and thus are key regulators of endocytosis in eukaryotic cells. This role for dynamin proteins is especially crucial for the proper function of neurons, where they
Jared A. Talbot +3 more
doaj +1 more source