Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Appears in Networks 1

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

In-Edges 12

bp(GO:"microtubule polymerization") positiveCorrelation complex(GO:microtubule) View Subject | View Object

We concluded that FKBP52 inhibits the promotion of microtubule assembly by Tau. PubMed:20133804

p(HGNC:MAPT) directlyIncreases complex(GO:microtubule) View Subject | View Object

Tau protein plays a role in the extension and maintenance of neuronal processes through a direct association with microtubules. It is found in the axonal microtubules of mature neurons (Binder et al ., 1985) and in the axonlike elongated neurite processes synthesized by differentiating neurons in culture. To address this issue, three different tau protein fragments were synthesized in vitro: (a) the tau protein repeat domain (residues 237 to 367); (b) the amino terminal half of tau protein (residues 1-237) ; and (c) the carboxy terminal nonrepeat domain of tau protein (residues 358 to 430). From these results, we conclude the repeat domain contributes most of the binding energy for microtubules. PubMed:1918161

p(HGNC:MAPT) association complex(GO:microtubule) View Subject | View Object

The resulting MAP-decorated neurofilaments formed a viscous complex with microtubules, showing that some component of the MAPs mediated the association between the two filamentous organelles. PubMed:6543144

p(HGNC:MAPT) association complex(GO:microtubule) View Subject | View Object

ABaC binds directly to MTs through a site that encompasses its catalytic subunit and is distinct from its binding site for tau, and ABaC and tau bind to different domains on MTs. PubMed:10464280

p(HGNC:PPP2CA) association complex(GO:microtubule) View Subject | View Object

ABaC binds directly to MTs through a site that encompasses its catalytic subunit and is distinct from its binding site for tau, and ABaC and tau bind to different domains on MTs. 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

act(p(HGNC:HSPA8)) negativeCorrelation act(complex(GO:microtubule)) 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(HGNC:KIF5B) association complex(GO:microtubule) View Subject | View Object

These include the scaffold protein JNK interacting protein (JIP) that is involved in the linkage of cargos to the kinesin-I motor complex via KLC (25, 28–33).This complex is formed by the kinesin heavy chain (KIF5; previously termed KHC), which interacts with microtubules, and kinesin light chain (KLC), which mediates cargo linkage. In addition, scaffolding proteins are involved such as the JIP1 that binds to KLC (21). PubMed:19491104

p(HGNC:MAPT, frag("237_367")) directlyIncreases complex(GO:microtubule) View Subject | View Object

Tau protein plays a role in the extension and maintenance of neuronal processes through a direct association with microtubules. It is found in the axonal microtubules of mature neurons (Binder et al ., 1985) and in the axonlike elongated neurite processes synthesized by differentiating neurons in culture. To address this issue, three different tau protein fragments were synthesized in vitro: (a) the tau protein repeat domain (residues 237 to 367); (b) the amino terminal half of tau protein (residues 1-237) ; and (c) the carboxy terminal nonrepeat domain of tau protein (residues 358 to 430). From these results, we conclude the repeat domain contributes most of the binding energy for microtubules. PubMed:1918161

p(INTERPRO:"Heat shock protein 70 family") association complex(GO:microtubule) 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 9

complex(GO:microtubule) association p(HGNC:MAPT) View Subject | View Object

The resulting MAP-decorated neurofilaments formed a viscous complex with microtubules, showing that some component of the MAPs mediated the association between the two filamentous organelles. PubMed:6543144

complex(GO:microtubule) association p(HGNC:MAPT) View Subject | View Object

ABaC binds directly to MTs through a site that encompasses its catalytic subunit and is distinct from its binding site for tau, and ABaC and tau bind to different domains on MTs. PubMed:10464280

complex(GO:microtubule) association p(HGNC:KIF5B) View Subject | View Object

These include the scaffold protein JNK interacting protein (JIP) that is involved in the linkage of cargos to the kinesin-I motor complex via KLC (25, 28–33).This complex is formed by the kinesin heavy chain (KIF5; previously termed KHC), which interacts with microtubules, and kinesin light chain (KLC), which mediates cargo linkage. In addition, scaffolding proteins are involved such as the JIP1 that binds to KLC (21). PubMed:19491104

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

complex(GO:microtubule) association p(HGNC:PPP2CA) View Subject | View Object

ABaC binds directly to MTs through a site that encompasses its catalytic subunit and is distinct from its binding site for tau, and ABaC and tau bind to different domains on MTs. PubMed:10464280

act(complex(GO:microtubule)) directlyDecreases act(complex(SCOMP:"PP2A Complex")) View Subject | View Object

Thus, MTs inhibited the rate of tau dephosphorylation by ABaC. PubMed:10464280

act(complex(GO:microtubule)) negativeCorrelation act(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

complex(GO:microtubule) association p(INTERPRO:"Heat shock protein 70 family") 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

complex(GO:microtubule) positiveCorrelation bp(GO:"microtubule polymerization") View Subject | View Object

We concluded that FKBP52 inhibits the promotion of microtubule assembly by Tau. PubMed:20133804

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.