Wikipedia

Andrea Musacchio

Andrea Musacchio (born July 11, 1964)[1] is an Italian structural biologist. He is Max Planck director at the Institute of Molecular Physiology in Dortmund. He is also Honorary Professor at the Center for Medical Biotechnology at the University of Duisburg-Essen. He was named European Molecular Biology Organization member in 2009.[2]

Andrea Musacchio
Born
Andrea Musacchio

(1964-07-11) July 11, 1964 (age 59)
Rome, Italy
NationalityItalian
Alma materUniversity of Rome Tor Vergata, European Molecular Biology Laboratory
Scientific career
FieldsCrystallography
InstitutionsHarvard Medical School, European Institute of Oncology, Max Planck Institute for Molecular Physiology
Doctoral advisorMatti Saraste
Other academic advisorsGianni Cesareni

Education and career edit

Musacchio received a Laurea in Biology from the University of Rome Tor Vergata summa cum laude in 1990, and earned his Ph.D., summa cum laude, from the Heidelberg University in 1995 working at the European Molecular Biology Laboratory. For his postdoctoral studies he joined Stephen C. Harrison laboratory at the Harvard Medical School in Boston. In 1999 he returned to Italy to found his laboratory at the European Institute of Oncology in Milan, where he started working on mechanisms of cell division. He was a European Molecular Biology Organization Young Investigator from 2000-2004. Musacchio moved to Dortmund in 2011 to direct the Department of Mechanistic Cell Biology at the Max Planck Institute for Molecular Physiology[3]

Research edit

Musacchio approached structural biology during his Ph.D., contributing to the determination of the first crystallographic structures of the SH3[4] and PH[5] domains. During his post-doctoral training, he was involved in the determination of the clathrin triskelion structure,[6] one of the first studies combining X-ray crystallography and electron microscopy. As an independent scientist, his interests focused on the understanding of the molecular basis of mitosis, with emphasis on the spindle assembly checkpoint. Since the early days, Musacchio's lab adopted a multi-disciplinary approach merging structural biology, biochemistry and cellular biology, this way gaining comprehensive views on protein functions in living cells.[7] He is best known for his work on Mad1/Mad2 complexes,[8][9] which led to the formulation of the template model,[10] and for his contributions to the understanding of the role of the kinase Aurora B, Mps1 and Haspin in mitosis.[11][12][13][14] In 2008, the structure of the Ndc80 complex [15] set the foundation of a new line of his investigations on kinetochore assembly and attachment to microtubules[16][17][18]

Personal life edit

Musacchio spent his childhood in Rome, where he grew to be a strong supporter of A.S. Roma. He has started embracing Borussia Dortmund.

He is married and father of two boys.

References edit

  1. ^ "Musacchio, Andrea". www.mpg.de. Retrieved 2024-01-12.
  2. ^ 2009 EMBO Press Release Archived 2014-12-09 at the Wayback Machine
  3. ^ Musacchio A. (2012). "Andrea Musacchio". Current Biology. 22 (14): R552–R554. doi:10.1016/j.cub.2012.06.024. PMID 23012739.
  4. ^ Musacchio, A; Noble, M; Pauptit, R; Wierenga, R; Saraste, M (Oct 29, 1992). "Crystal structure of a Src-homology 3 (SH3) domain". Nature. 359 (6398): 851–5. Bibcode:1992Natur.359..851M. doi:10.1038/359851a0. PMID 1279434. S2CID 4254768.
  5. ^ Macias, MJ; Musacchio, A; Ponstingl, H; Nilges, M; Saraste, M; Oschkinat, H (Jun 23, 1994). "Structure of the pleckstrin homology domain from beta-spectrin". Nature. 369 (6482): 675–7. Bibcode:1994Natur.369..675M. doi:10.1038/369675a0. PMID 8208297. S2CID 4358947.
  6. ^ Musacchio, A; Smith, CJ; Roseman, AM; Harrison, SC; Kirchhausen, T; Pearse, BM (Jun 1999). "Functional Organization of Clathrin in Coats: Combining Electron Cryomicroscopy and X-Ray Crystallography". Molecular Cell. 3 (6): 761–70. doi:10.1016/S1097-2765(01)80008-3. PMID 10394364.
  7. ^ Nasmyth, K (Mar 25, 2005). "How do so few control so many?". Cell. 120 (6): 739–46. doi:10.1016/j.cell.2005.03.006. PMID 15797376. S2CID 18831437.
  8. ^ Sironi, L; Mapelli, M; Knapp, S; De Antoni, A; Jeang, KT; Musacchio, A (May 15, 2002). "Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint". The EMBO Journal. 21 (10): 2496–506. doi:10.1093/emboj/21.10.2496. PMC 126000. PMID 12006501.
  9. ^ Mapelli, M; Massimiliano, L; Santaguida, S; Musacchio, A (Nov 16, 2007). "The Mad2 conformational dimer: structure and implications for the spindle assembly checkpoint" (PDF). Cell. 131 (4): 730–43. doi:10.1016/j.cell.2007.08.049. hdl:2434/65744. PMID 18022367. S2CID 17345925.
  10. ^ De Antoni, A; Pearson, CG; Cimini, D; Canman, JC; Sala, V; Nezi, L; Mapelli, M; Sironi, L; Faretta, M; Salmon, ED; Musacchio, A (Feb 8, 2005). "The Mad1/Mad2 complex as a template for Mad2 activation in the spindle assembly checkpoint". Current Biology. 15 (3): 214–25. doi:10.1016/j.cub.2005.01.038. PMID 15694304. S2CID 3224122.
  11. ^ De Antoni, A; Maffini, S; Knapp, S; Musacchio, A; Santaguida, S (Oct 15, 2012). "A small-molecule inhibitor of Haspin alters the kinetochore functions of Aurora B." (PDF). The Journal of Cell Biology. 199 (2): 269–84. doi:10.1083/jcb.201205119. PMC 3471222. PMID 23071153.
  12. ^ Santaguida, S; Vernieri, C; Villa, F; Ciliberto, A; Musacchio, A (Apr 20, 2011). "Evidence that Aurora B is implicated in spindle checkpoint signalling independently of error correction". The EMBO Journal. 30 (8): 1508–19. doi:10.1038/emboj.2011.70. PMC 3102279. PMID 21407176.
  13. ^ Santaguida, S; Tighe, A; D'Alise, AM; Taylor, SS; Musacchio, A (Jul 12, 2010). "Dissecting the role of MPS1 in chromosome biorientation and the spindle checkpoint through the small molecule inhibitor reversine". The Journal of Cell Biology. 190 (1): 73–87. doi:10.1083/jcb.201001036. PMC 2911657. PMID 20624901.
  14. ^ Sessa, F; Mapelli, M; Ciferri, C; Tarricone, C; Areces, LB; Schneider, TR; Stukenberg, PT; Musacchio, A (Apr 29, 2005). "Mechanism of Aurora B activation by INCENP and inhibition by hesperadin". Molecular Cell. 18 (3): 379–91. doi:10.1016/j.molcel.2005.03.031. PMID 15866179.
  15. ^ Ciferri, C; Pasqualato, S; Screpanti, E; Varetti, G; Santaguida, S; Dos Reis, G; Maiolica, A; Polka, J; De Luca, JG; De Wulf, P; Salek, M; Rappsilber, J; Moores, CA; Salmon, ED; Musacchio, A (May 2, 2008). "Implications for kinetochore-microtubule attachment from the structure of an engineered Ndc80 complex". Cell. 133 (3): 427–39. doi:10.1016/j.cell.2008.03.020. PMC 4754795. PMID 18455984.
  16. ^ Santaguida, S; Musacchio, A (Sep 2, 2009). "The life and miracles of kinetochores". The EMBO Journal. 28 (17): 2511–31. doi:10.1038/emboj.2009.173. PMC 2722247. PMID 19629042.
  17. ^ Petrovic, A; Mosalaganti, S; Keller, J; Mattiuzzo, M; Overlack, K; Krenn, V; De Antoni, A; Wohlgemuth, S; Cecatiello, V; Pasqualato, S; Raunser, S; Musacchio, A (Feb 20, 2014). "Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization". Molecular Cell. 53 (4): 591–605. doi:10.1016/j.molcel.2014.01.019. hdl:10281/397721. PMID 24530301.
  18. ^ Basilico, F; Maffini, S; Weir, JR; Prumbaum, D; Rojas, AM; Zimniak, T; De Antoni, A; Jeganethan, S; Voss, B; van Gerwen, S; Krenn, V; Massimiliano, L; Valencia, A; Vetter, IR; Herzog, F; Raunser, S; Pasqualato, S; Musacchio, A (Jul 8, 2014). "The pseudo GTPase CENP-M drives human kinetochore assembly". eLife. 3: e02978. doi:10.7554/elife.02978. PMC 4080450. PMID 25006165.

External links edit

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