complex(GO:microtubule)

Entity

Name

microtubule

Namespace

go

Namespace Version

20180921

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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