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Entity

Name
microtubule-binding region
Namespace
HBP
Namespace Version
20190207
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/cf4d8bb88754f036b943b4d94ad96e103dcb7149/export/hbp-names.belns

Appears in Networks 2

In-Edges 7

p(HGNC:HDAC6) association p(HBP:"microtubule-binding region") View Subject | View Object

Apart from binding to MT, the repeat domains of tau also bind to tubulin deacetylase, histone deacetylase 6 (HDAC6) [68] and apolipoprotein E (apoE) more with the PubMed:26751493

act(complex(GO:microtubule)) positiveCorrelation p(HBP:"microtubule-binding region") View Subject | View Object

Using tau deletion mutants, we found that ABaC binds a domain on tau that is indistinguishable from its MT-binding domain. PubMed:10464280

act(complex(SCOMP:"PP2A Complex")) association p(HBP:"microtubule-binding region") View Subject | View Object

Using tau deletion mutants, we found that ABaC binds a domain on tau that is indistinguishable from its MT-binding domain. PubMed:10464280

p(FPLX:Ubiquitin) association p(HBP:"microtubule-binding region") View Subject | View Object

The ubiquitin-targeted protein was identified as tau in paired helical filaments, and the conjugation sites were localized to the microtubule-binding region. PubMed:8391280

p(HGNC:HSPA8) association p(HBP:"microtubule-binding region") View Subject | View Object

The location of the hsc70-binding site in the tau MTBR suggests that hsc70 cannot bind microtubule-associated tau. The location of the hsc70-binding site also suggests that hsc70 might compete with tubulin or microtubules for binding to tau. Our data implicating I308/V309 in tau’s binding to hsp70 similarly suggest that tau cannot bind simultaneously to hsp70 and microtubules. However, unlike hsc70, which does not associate directly with tubulin or microtubules (Gache et al. 2005), hsp70 binds microtubules, presumably through its N-terminus (Sanchez et al. 1994). This would allow hsp70 to simultaneously bind to tau through its C-terminal substrate-binding domain and to microtubules through its N-terminus. PubMed:18500754

p(INTERPRO:"Heat shock protein 70kD, C-terminal domain superfamily") association p(HBP:"microtubule-binding region") View Subject | View Object

The location of the hsc70-binding site in the tau MTBR suggests that hsc70 cannot bind microtubule-associated tau. The location of the hsc70-binding site also suggests that hsc70 might compete with tubulin or microtubules for binding to tau. Our data implicating I308/V309 in tau’s binding to hsp70 similarly suggest that tau cannot bind simultaneously to hsp70 and microtubules. However, unlike hsc70, which does not associate directly with tubulin or microtubules (Gache et al. 2005), hsp70 binds microtubules, presumably through its N-terminus (Sanchez et al. 1994). This would allow hsp70 to simultaneously bind to tau through its C-terminal substrate-binding domain and to microtubules through its N-terminus. PubMed:18500754

Out-Edges 8

p(HBP:"microtubule-binding region") association p(HGNC:HDAC6) View Subject | View Object

Apart from binding to MT, the repeat domains of tau also bind to tubulin deacetylase, histone deacetylase 6 (HDAC6) [68] and apolipoprotein E (apoE) more with the PubMed:26751493

p(HBP:"microtubule-binding region") association act(complex(SCOMP:"PP2A Complex")) View Subject | View Object

Using tau deletion mutants, we found that ABaC binds a domain on tau that is indistinguishable from its MT-binding domain. PubMed:10464280

p(HBP:"microtubule-binding region") positiveCorrelation act(complex(GO:microtubule)) View Subject | View Object

Using tau deletion mutants, we found that ABaC binds a domain on tau that is indistinguishable from its MT-binding domain. PubMed:10464280

p(HBP:"microtubule-binding region") association p(HGNC:HSPA8) View Subject | View Object

The location of the hsc70-binding site in the tau MTBR suggests that hsc70 cannot bind microtubule-associated tau. The location of the hsc70-binding site also suggests that hsc70 might compete with tubulin or microtubules for binding to tau. Our data implicating I308/V309 in tau’s binding to hsp70 similarly suggest that tau cannot bind simultaneously to hsp70 and microtubules. However, unlike hsc70, which does not associate directly with tubulin or microtubules (Gache et al. 2005), hsp70 binds microtubules, presumably through its N-terminus (Sanchez et al. 1994). This would allow hsp70 to simultaneously bind to tau through its C-terminal substrate-binding domain and to microtubules through its N-terminus. PubMed:18500754

p(HBP:"microtubule-binding region") association p(INTERPRO:"Heat shock protein 70kD, C-terminal domain superfamily") View Subject | View Object

The location of the hsc70-binding site in the tau MTBR suggests that hsc70 cannot bind microtubule-associated tau. The location of the hsc70-binding site also suggests that hsc70 might compete with tubulin or microtubules for binding to tau. Our data implicating I308/V309 in tau’s binding to hsp70 similarly suggest that tau cannot bind simultaneously to hsp70 and microtubules. However, unlike hsc70, which does not associate directly with tubulin or microtubules (Gache et al. 2005), hsp70 binds microtubules, presumably through its N-terminus (Sanchez et al. 1994). This would allow hsp70 to simultaneously bind to tau through its C-terminal substrate-binding domain and to microtubules through its N-terminus. PubMed:18500754

p(HBP:"microtubule-binding region") association p(FPLX:Ubiquitin) View Subject | View Object

The ubiquitin-targeted protein was identified as tau in paired helical filaments, and the conjugation sites were localized to the microtubule-binding region. PubMed:8391280

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.