Trends in Cell Biology
Volume 9, Issue 3, 1 March 1999, Pages 96-102
Journal home page for Trends in Cell Biology

Review
Functional diversity in the dynamin family

https://doi.org/10.1016/S0962-8924(98)01490-1Get rights and content

Abstract

The function of the GTPase dynamin has been discussed for several years. It clearly plays a role in vesicle budding, but, despite recent insights, precisely how it functions in this process is still a matter of debate. In addition, it is now clear that dynamin is a member of a large protein family, present in a variety of cellular locations where members apparently perform a range of functions. This article describes current understanding of the structure and function of the various dynamin family members.

Section snippets

The primary function of dynamin

The question concerning whether dynamin actively pinches off vesicles or, alternatively, has a regulatory function has been discussed in this journal before10. The prevailing view that dynamin severs membrane started with the observation that concentrated dynamin can spontaneously form spirals without the need for other proteins or membrane11. Some of these spirals appeared partially constricted, thereby suggesting that dynamin drives scission. Furthermore, nerve endings incubated with GTPγS

Different dynamins, different binding partners

Drosophila and C. elegans each appear to have only one gene encoding dynamin, which is expressed at high levels in neurons but is also essential for endocytosis in non-neuronal tissues2. By contrast, mammals have three dynamin isoforms – with different expression patterns and possibly different functions27. Dynamin 1 is expressed at high levels in brain, where it could be dedicated to recycling synaptic vesicles. Dynamin 2 is expressed ubiquitously, most probably facilitating receptor-mediated

An emerging family of dynamin-related proteins

Increasing numbers of dynamin-related proteins have appeared in the literature. The functions of many of these family members are still a matter of debate (Box 1). However, data from the three most extensively sequenced species (yeast, C. elegans and human) suggest that eukaryotes share three basic classes of dynamin-related proteins (Fig. 2). The first class contains dynamin-like proteins involved in vesicular traffic: in yeast, Vps1p41; in C. elegans, dyn-12; and, in mammals, dynamins 1, 2

Common features of dynamin-related proteins

The dynamin family members are characterized by their common structure and by conserved sequences in the GTP-binding domain. The GTPase, which is approximately 300 amino acids, is always followed by a middle domain of approximately 150 amino acids and an assembly domain of approximately 100 amino acids (Fig. 1). The assembly domains typically have a propensity to form coiled coils, and, in Mx proteins, this domain has leucine zippers. Genuine dynamins have a PH domain between the middle and the

Concluding remarks

We will undoubtedly learn much more about the functions of the dynamin family members, and it looks as though dynamin itself will continue to lead the way. That there are similar arrangements of protein domains suggests that different dynamin family members use similar mechanisms. Future studies with purified proteins might reveal whether all family members form spirals. Their primary functions have proved more difficult to determine. Do the functions that we already know have a common theme or

Acknowledgements

I thank Greg Payne, Arnaud Labrousse, Elena Smirnova, Dan Rube and Dixie-Lee Shurland for their helpful suggestions and Sabrina Dyall for help with the phylogenetic tree. This work was supported by grants from the NIH (GM 51866), the American Heart Association and the Cancer Research Coordinating Committee. My apologies to all whose work I was unable to cite owing to lack of space.

References (64)

  • H.S. Shpetner et al.

    Cell

    (1989)
  • S.L. Schmid et al.

    Curr. Opin. Cell Biol.

    (1998)
  • S.M. Sweitzer et al.

    Cell

    (1998)
  • K. Takei

    Cell

    (1998)
  • D.E. Warnock et al.

    J. Biol. Chem.

    (1996)
  • J.F. Carr et al.

    J. Biol. Chem.

    (1997)
  • H. Kuromi et al.

    Neuron

    (1998)
  • D. Grabs

    J. Biol. Chem.

    (1997)
  • A. Volchuk

    J. Biol. Chem.

    (1998)
  • B. Barylko

    J. Biol. Chem.

    (1998)
  • H.C. Lin

    J. Biol. Chem.

    (1997)
  • H.C. Lin et al.

    J. Biol. Chem.

    (1996)
  • S. Floyd et al.

    Trends Cell Biol.

    (1998)
  • J. Roos et al.

    J. Biol. Chem.

    (1998)
  • J.H. Rothman

    Cell

    (1990)
  • M. Nakayama

    J. Biol. Chem.

    (1993)
  • M. Schwemmle

    J. Biol. Chem.

    (1995)
  • B. Schumacher et al.

    J. Biol. Chem.

    (1998)
  • M.F. Richter

    J. Biol. Chem.

    (1995)
  • T.A. Grigliatti

    Mol. Gen. Genet.

    (1973)
  • S.G. Clark

    Proc. Natl. Acad. Sci. U. S. A.

    (1997)
  • T. Kosaka et al.

    J. Neurobiol.

    (1983)
  • A.M. van der Bliek et al.

    Nature

    (1991)
  • M.S. Chen

    Nature

    (1991)
  • A.M. van der Bliek

    J. Cell Biol.

    (1993)
  • J.S. Herskovits

    J. Cell Biol.

    (1993)
  • J. Roos et al.

    Trends Cell Biol.

    (1997)
  • J.E. Hinshaw et al.

    Nature

    (1995)
  • K. Takei

    Nature

    (1995)
  • J.P. Liu et al.

    Science

    (1994)
  • V.I. Slepnev

    Science

    (1998)
  • P. Oh et al.

    J. Cell Biol.

    (1998)
  • Cited by (228)

    • Myxovirus resistance 1 (Mx1) gene: Molecular characterization of complete coding sequence and expression profile in the endometrium of goat (Capra hircus)

      2021, Journal of Reproductive Immunology
      Citation Excerpt :

      The GED domain supports intra-molecular activation of GTP and the C-terminal leucine zippers in-between positions of 590 to 649 amino acids in the GED, fold back to join the N-terminal GTP-binding domain and form a functional center of Mx proteins (Lee et al., 2000). The C-terminal leucine zippers also allow self-assembling into higher-order structures that resemble rings and helical stacks of rings (Van der Bliek, 1999). The cpMx1 protein structure showed that the conserved residues Thr98, Pro91, Gly95, Asp173, Gly95, Gln74, Ser76, Gly277, Lys243, Cys275, Thr242, Arg276, Ser75, Gly93, Leu90, Val273 are essential for tight anchoring of GTP within the binding cavity of G-domain (Das et al., 2019).

    • Physiological and biochemical perspectives of non-salt tolerant plants during bacterial interaction against soil salinity

      2017, Plant Physiology and Biochemistry
      Citation Excerpt :

      An increased level of glycolysis-related proteins in salt affected plants associated with bacterial colonies reflects the acclimation to salt stress. ADL1 genes code dynamin-like proteins and guanosine triphosphate (GTP)-binding proteins (Van-der-Bliek, 1999) in Arabidopsis and are involved in vesicular trafficking and cytokinesis in embryogenesis, seedling development, and reproduction (Kang et al., 2001). Similarly, ADL2 genes participate in mitochondrial division (Arimura et al., 2004).

    View all citing articles on Scopus
    View full text