Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | R411-R416 |
| Journal | Current Biology |
| Volume | 28 |
| Issue number | 8 |
| DOIs | |
| State | Published - Apr 23 2018 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)
Cite this
The dynamin superfamily. / Ramachandran, Rajesh; Schmid, Sandra L.
In: Current Biology, Vol. 28, No. 8, 23.04.2018, p. R411-R416.Research output: Contribution to journal › Short survey
}
TY - JOUR
T1 - The dynamin superfamily
AU - Ramachandran, Rajesh
AU - Schmid, Sandra L.
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.
UR - http://www.scopus.com/inward/record.url?scp=85045769611&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85045769611&partnerID=8YFLogxK
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 -