Michel Steinmetz

Prof. Michel Steinmetz


Research Focus & Metrics

Academic Career Length

31Years (1996-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 July 2009 in Cell
Verified
Journal Article
Closed access
SHSrinivas Honnappa
Srinivas Honnappa
SGSusana Montenegro Gouveia
Susana Montenegro Gouveia
AWAnke Weisbrich
Anke Weisbrich
FDFred F. Damberger
Fred F. Damberger
Neel Sarovar BhaveshNeel Sarovar Bhavesh
Neel Sarovar Bhavesh
MSMichel Steinmetz
Michel Steinmetz

1 May 2005 in Nature
Verified
Journal Article
Closed access
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BGBenoît Gigant
Benoît Gigant
CWChunguang Wang
Chunguang Wang
RRRaimond Ravelli
Raimond Ravelli
FRFanny Roussi
Fanny Roussi
MSMichel Steinmetz
Michel Steinmetz
MKMarcel Knossow
Marcel Knossow

1 February 2008 in Current Biology
Verified
Journal Article
Closed access
IGIlya Grigoriev
Ilya Grigoriev
SGSusana Montenegro Gouveia
Susana Montenegro Gouveia
BVBabet van der Vaart
Babet van der Vaart
Jeroen A. A. DemmersJeroen A. A. Demmers
Jeroen A. A. Demmers
JSJeremy T. Smyth
Jeremy T. Smyth
AAAnna Akhmanova
Anna Akhmanova

1 February 2013 in Science
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Journal Article
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APAndrea E. Prota
Andrea E. Prota
KBKatja Bargsten
Katja Bargsten
DZDidier Zurwerra
Didier Zurwerra
JFJessica J. Field
Jessica J. Field
JJosé Fernando Díaz
José Fernando Díaz
MSMichel Steinmetz
Michel Steinmetz
Dissecting Microtubule Stability: Microtubule-stabilizing agents (MSAs), like taxol, inhibit cell division and are widely used in cancer chemotherapy. Prota et al. (p. 587 , published online 3 January) present structural data on the molecular mechanism of action of antimitotic drugs. Tubulin structures in complex with the MSAs zampanolide and epothilone A, revealed a general mechanism for how MSAs promote microtubule assembly and stability by affecting lateral tubulin interactions.

1 February 2011 in Cell
Verified
Journal Article
Open access
DKDaiju Kitagawa
Daiju Kitagawa
IVIoannis Vakonakis
Ioannis Vakonakis
NONatacha Olieric
Natacha Olieric
MHManuel Hilbert
Manuel Hilbert
DKDebora Keller
Debora Keller
MSMichel Steinmetz
Michel Steinmetz
The centriole, and the related basal body, is an ancient organelle characterized by a universal 9-fold radial symmetry and is critical for generating cilia, flagella, and centrosomes. The mechanisms directing centriole formation are incompletely understood and represent a fundamental open question in biology. Here, we demonstrate that the centriolar protein SAS-6 forms rod-shaped homodimers that interact through their N-terminal domains to form oligomers. We establish that such oligomerization is essential for centriole formation in C. elegans and human cells. We further generate a structural model of the related protein Bld12p from C. reinhardtii, in which nine homodimers assemble into a ring from which nine coiled-coil rods radiate outward. Moreover, we demonstrate that recombinant Bld12p self-assembles into structures akin to the central hub of the cartwheel, which serves as a scaffold for centriole formation. Overall, our findings establish a structural basis for the universal 9-fold symmetry of centrioles.

1 October 2018 in Trends in Cell Biology
Verified
Journal Article
Closed access
MSMichel Steinmetz
Michel Steinmetz
APAndrea E. Prota
Andrea E. Prota