Dataset Information

Identification of microtubule associated proteins

ABSTRACT: To find out the identities of microtubule-associated proteins whose abundances are visibly reduced in presence of Taxol. For this experiment, microtubule-associated proteins are pulleddown after treatment with Taxol. Untreated cells are used as a control.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Saikat Chakraborty

LAB HEAD: Prof. Wolfgang Baumeister

PROVIDER: PXD035700 | Pride | 2025-05-06

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20161111_coreQEP1_NaNa_SA_Orbi2365Sample01.raw	Raw
	20161111_coreQEP1_NaNa_SA_Orbi2365Sample02.raw	Raw
	20161111_coreQEP1_NaNa_SA_Orbi2365Sample03.raw	Raw
	20161111_coreQEP1_NaNa_SA_Orbi2365Sample04.raw	Raw
	20161111_coreQEP1_NaNa_SA_Orbi2365Sample05.raw	Raw

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Publications

Cryo-ET suggests tubulin chaperones form a subset of microtubule lumenal particles with a role in maintaining neuronal microtubules.

Chakraborty Saikat S Martinez-Sanchez Antonio A Beck Florian F Toro-Nahuelpan Mauricio M Hwang In-Young IY Noh Kyung-Min KM Baumeister Wolfgang W Mahamid Julia J

Proceedings of the National Academy of Sciences of the United States of America 20250131 5

The functional architecture of the long-lived neuronal microtubule (MT) cytoskeleton is maintained by various MT-associated proteins (MAPs), most of which are known to bind to the MT outer surface. However, electron microscopy (EM) has long ago revealed the presence of particles inside the lumens of neuronal MTs, of yet unknown identity and function. Here, we use cryogenic electron tomography (cryo-ET) to analyze the three-dimensional (3D) organization and structures of MT lumenal particles in p ...[more]

PMID: 39888918

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