Amino Acids

, Volume 41, Issue 2, pp 363–385 | Cite as

Proteome analysis of microtubule-associated proteins and their interacting partners from mammalian brain

  • Frank Kozielski
  • Tahira Riaz
  • Salvatore DeBonis
  • Christian J. Koehler
  • Mario Kroening
  • Isabel Panse
  • Margarita Strozynski
  • Ian M. Donaldson
  • Bernd ThiedeEmail author
Original Article


The microtubule (MT) cytoskeleton is essential for a variety of cellular processes. MTs are finely regulated by distinct classes of MT-associated proteins (MAPs), which themselves bind to and are regulated by a large number of additional proteins. We have carried out proteome analyses of tubulin-rich and tubulin-depleted MAPs and their interacting partners isolated from bovine brain. In total, 573 proteins were identified giving us unprecedented access to brain-specific MT-associated proteins from mammalian brain. Most of the standard MAPs were identified and at least 500 proteins have been reported as being associated with MTs. We identified protein complexes with a large number of subunits such as brain-specific motor/adaptor/cargo complexes for kinesins, dynein, and dynactin, and proteins of an RNA-transporting granule. About 25% of the identified proteins were also found in the synaptic vesicle proteome. Analysis of the MS/MS data revealed many posttranslational modifications, amino acid changes, and alternative splice variants, particularly in tau, a key protein implicated in Alzheimer’s disease. Bioinformatic analysis of known protein–protein interactions of the identified proteins indicated that the number of MAPs and their associated proteins is larger than previously anticipated and that our database will be a useful resource to identify novel binding partners.


Alternative splice variants Brain MAPs Posttranslational modifications Protein–protein interactions 



Adenylyl 5′-(β,γ-methylene)diphosphonate


Adenosine triphosphate


Ethylenediaminetetraacetic acid


Guanosine triphosphate


Kinesin light chain


Microtubule-associated proteins


Rac GTPase-activating protein 1


Mitotic kinesin-like protein 1




1,4-Piperazinediethanesulfonic acid




Synaptic vesicle protein


N α -p-Tosyl-l-arginine methyl ester

Supplementary material

726_2010_649_MOESM1_ESM.pdf (5.1 mb)
Supplementary figure 1 (PDF 5191 kb)
726_2010_649_MOESM2_ESM.pdf (3 mb)
Supplementary figure 2 (PDF 3030 kb)
726_2010_649_MOESM3_ESM.xls (6.4 mb)
Supplementary tables 1–10 (XLS 6569 kb)
726_2010_649_MOESM4_ESM.xls (798 kb)
Supplementary tables 11–15 (XLS 798 kb)


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Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  • Frank Kozielski
    • 1
  • Tahira Riaz
    • 2
  • Salvatore DeBonis
    • 3
  • Christian J. Koehler
    • 2
  • Mario Kroening
    • 2
  • Isabel Panse
    • 2
  • Margarita Strozynski
    • 2
  • Ian M. Donaldson
    • 2
  • Bernd Thiede
    • 2
    • 4
    Email author
  1. 1.The Beatson Institute for Cancer ResearchGlasgowScotland, UK
  2. 2.The Biotechnology Centre of OsloUniversity of OsloOsloNorway
  3. 3.Institut de Biologie Structurale (CEA-CNRS-UJF)Grenoble Cedex 01France
  4. 4.The Biotechnology Centre of OsloUniversity of OsloOsloNorway

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