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PRR of Tau Crosslinking with Tubulin

ABSTRACT: We used cross-linking mass spectrometry with the cleavable cross-linker, disuccinimidyl dibutyric urea (DSBU) to map sites of interaction between the proline rich domain (PRR, tau amino acids 149-244) and tubulin. For comparison, we also conducted these experiments with PRR constructs containing multiple phosphomimic mutations (from serine or threonine to glutamate) at tau amino acid positions 181, 217, 231 and 235.

INSTRUMENT(S):

ORGANISM(S): Bos Taurus (bovine) Escherichia Coli

SUBMITTER: Hee Jong Kim

LAB HEAD: Kenji Murakami

PROVIDER: PXD049384 | Pride | 2026-03-09

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20220824_tau_Mut_et_al_DE3_BOVIN.fasta	Fasta
	20220824_tau_WT_et_al_DE3_BOVIN.fasta	Fasta
	20221022_4xMut_bottom_dsbu_combined_comprehensive.tsv	Tabular
	20221022_4xMut_top_dsbu_combined_comprehensive.tsv	Tabular
	20221022_PRR_bottom_dsbu_combined_comprehensive.tsv	Tabular

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Publications

Structural insights into the role of the proline rich region in tau function.

Acosta Karen K Brue Christopher R CR Holubovska Polina P Kim Hee Jong HJ Mayne Leland L Murakami Kenji K Rhoades Elizabeth E

Structure (London, England : 1993) 20250117 3

Tau plays an important role in modulating axonal microtubules in neurons, while intracellular tau aggregates are found in many neurodegenerative disorders. Tubulin binding sites are found in tau's proline-rich region (PRR), microtubule binding repeats (MTBRs), and pseudo-repeat (R'). Tau phosphorylation sites, which cluster with high frequency within the PRR, regulate tubulin interactions and correlates with disease. Here, we use fluorescence correlation spectroscopy and structural mass spectrom ...[more]

PMID: 39826549

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