TY - JOUR
T1 - The dynamin superfamily
AU - Ramachandran, Rajesh
AU - Schmid, Sandra L.
N1 - Publisher Copyright:
© 2018 Elsevier Ltd
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 2018/4/23
Y1 - 2018/4/23
N2 - The dynamin superfamily comprises a growing assortment of multi-domain GTPases, found from bacteria to man, that are distinguished from typical GTPases of the Ras, Rab and G-protein families by their modular structure (Figure 1), relatively large size (>70 kDa), and low affinity for guanine nucleotides. In addition, they display a conserved propensity to self-assemble into polymeric arrays, the dynamics of which are regulated by an autonomous, assembly-stimulated GTPase activity. Here, Ramachandran and Schmid describe the structural, biophysical, and biochemical properties of the dynamin superfamily and the implications for their distinct cellular functions.
AB - The dynamin superfamily comprises a growing assortment of multi-domain GTPases, found from bacteria to man, that are distinguished from typical GTPases of the Ras, Rab and G-protein families by their modular structure (Figure 1), relatively large size (>70 kDa), and low affinity for guanine nucleotides. In addition, they display a conserved propensity to self-assemble into polymeric arrays, the dynamics of which are regulated by an autonomous, assembly-stimulated GTPase activity. Here, Ramachandran and Schmid describe the structural, biophysical, and biochemical properties of the dynamin superfamily and the implications for their distinct cellular functions.
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U2 - 10.1016/j.cub.2017.12.013
DO - 10.1016/j.cub.2017.12.013
M3 - Short survey
C2 - 29689225
AN - SCOPUS:85045769611
VL - 28
SP - R411-R416
JO - Current Biology
JF - Current Biology
SN - 0960-9822
IS - 8
ER -