The dynamin superfamily

Rajesh Ramachandran; Sandra L. Schmid

doi:10.1016/j.cub.2017.12.013

The dynamin superfamily

Rajesh Ramachandran, Sandra L. Schmid

Research output: Contribution to journal › Short survey › peer-review

58 Scopus citations

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	https://doi.org/10.1016/j.cub.2017.12.013
State	Published - Apr 23 2018

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Agricultural and Biological Sciences(all)

Access to Document

10.1016/j.cub.2017.12.013

Cite this

@article{4921c24d71f14dea8c6fa2714ce36316,

title = "The dynamin superfamily",

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.",

author = "Rajesh Ramachandran and Schmid, {Sandra L.}",

note = "Publisher Copyright: {\textcopyright} 2018 Elsevier Ltd",

year = "2018",

month = apr,

day = "23",

doi = "10.1016/j.cub.2017.12.013",

language = "English (US)",

volume = "28",

pages = "R411--R416",

journal = "Current Biology",

issn = "0960-9822",

publisher = "Cell Press",

number = "8",

}

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 -

The dynamin superfamily

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this