Results 11 to 20 of about 41,917 (266)

Phosphorylation of dynamin by ERK2 inhibits the dynamin‐microtubule interaction [PDF]

open access: yesFEBS 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   +3 more sources

Dynamin 1 is required for memory formation. [PDF]

open access: yesPLoS 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   +3 more sources

SNARE Filtering by Dynamin [PDF]

open access: yesCell, 2004
Fission and fusion are the two elementary steps of membrane traffic. The mechanoenzyme dynamin acts at the fission step, but, in this issue of Cell, suggest an additional role of dynamin in preparing membranes for fusion.
Antonny, B., Antonny, Bruno
openaire   +3 more sources

Kalirin12 interacts with dynamin [PDF]

open access: yesBMC Neuroscience, 2009
Abstract Background Guanine nucleotide exchange factors (GEFs) and their target Rho GTPases regulate cytoskeletal changes and membrane trafficking. Dynamin, a large force-generating GTPase, plays an essential role in membrane tubulation and fission in cells. Kalirin12, a neuronal RhoGEF, is found in growth cones early
Mains Richard E   +3 more
openaire   +4 more sources

Dynamin Subunit Interactions Revealed [PDF]

open access: yesDevelopmental 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   +3 more sources

Redundant and Distinct Functions for Dynamin-1 and Dynamin-2 Isoforms [PDF]

open access: yesThe Journal of Cell Biology, 1998
A role for dynamin in clathrin-mediated endocytosis is now well established. However, mammals express three closely related, tissue-specific dynamin isoforms, each with multiple splice variants. Thus, an important question is whether these isoforms and splice variants function in vesicle formation from distinct intracellular organelles.
Altschuler, Yoram   +6 more
openaire   +5 more sources

A Corkscrew Model for Dynamin Constriction [PDF]

open access: yesStructure, 2007
Numerous vesiculation processes throughout the eukaryotic cell are dependent on the protein dynamin, a large GTPase that constricts lipid bilayers. We have combined X-ray crystallography and cryo-electron microscopy (cryo-EM) data to generate a coherent model of dynamin-mediated membrane constriction.
Mears, Jason A.   +2 more
openaire   +3 more sources

Dynamin inhibitors block activation of mTORC1 by amino acids independently of dynamin [PDF]

open access: yesJournal of Cell Science, 2018
ABSTRACT mTORC1 plays a crucial role in protein synthesis and cell proliferation and growth. It is activated by growth factors and amino acids, including essential amino acids (EAAs), such as leucine; Leu enters cells via the Leu transporter LAT1–4F2hc (also known as SLC7A5–SLC3A2) and potentially via endocytosis.
Avinash Persaud   +3 more
openaire   +3 more sources

Mapping of Tilapia Lake Virus entry pathways with inhibitors reveals dependence on dynamin activity and cholesterol but not endosomal acidification

open access: yesFrontiers in Cell and Developmental Biology, 2022
Tilapia Lake Virus (TiLV) is an emerging virus lethal to tilapia, which threatens the global tilapia aquaculture with severe implications for food security.
Reem Abu Rass   +5 more
doaj   +1 more source

Dynamins at a glance [PDF]

open access: yesJournal of Cell Science, 2009
The superfamily of dynamins includes classical dynamins and dynamin-related proteins. Classical dynamins are proteins that share sequence similarity with the first described dynamin, which is a large GTPase with five characteristic domains.
Jürgen A W, Heymann, Jenny E, Hinshaw
openaire   +2 more sources

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