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Mass spectrometric analysis of microtubule co‐sedimented proteins from rat brain
Author(s) -
Sakamoto Tatsuhiko,
Uezu Akiyoshi,
Kawauchi Shinya,
Kuramoto Takuya,
Makino Koji,
Umeda Kazuaki,
Araki Norie,
Baba Hideo,
Nakanishi Hiroyuki
Publication year - 2008
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2008.01175.x
Subject(s) - biology , centrosome , microtubule , microbiology and biotechnology , cytoskeleton , tubulin , vesicular transport protein , golgi apparatus , biochemistry , vesicle , cell , cell cycle , endoplasmic reticulum , membrane
Microtubules (MTs) play crucial roles in a variety of cell functions, such as mitosis, vesicle transport and cell motility. MTs also compose specialized structures, such as centrosomes, spindles and cilia. However, molecular mechanisms of these MT‐based functions and structures are not fully understood. Here, we analyzed MT co‐sedimented proteins from rat brain by tandem mass spectrometry (MS) upon ion exchange column chromatography. We identified a total of 391 proteins. These proteins were grouped into 12 categories: 57 MT cytoskeletal proteins, including MT‐associated proteins (MAPs) and motor proteins; 66 other cytoskeletal proteins; 4 centrosomal proteins; 10 chaperons; 5 Golgi proteins; 7 mitochondrial proteins; 62 nucleic acid‐binding proteins; 14 nuclear proteins; 13 ribosomal proteins; 28 vesicle transport proteins; 83 proteins with diverse function and/or localization; and 42 uncharacterized proteins. Of these uncharacterized proteins, six proteins were expressed in cultured cells, resulting in the identification of three novel components of centrosomes and cilia. Our present method is not specific for MAPs, but is useful for identifying low abundant novel MAPs and components of MT‐based structures. Our analysis provides an extensive list of potential candidates for future study of the molecular mechanisms of MT‐based functions and structures.