+ |
PRKCQ | up-regulates activity
phosphorylation
|
WIPF1 |
0.328 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249181 |
Ser488 |
RNESRSGsNRRERGA |
in vitro |
|
pmid |
sentence |
12504004 |
TCR engagement also causes PKCtheta-dependent phosphorylation of WIP, causing the disengagement of WASP from the WIP-WASP complex, thereby releasing it from WIP inhibition. These results suggest that the ZAP-70-CrkL-WIP pathway and PKCtheta link TCR to WASP activation. | These results suggest that phosphorylation at S488 disrupts WIP binding to WASP. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
WIPF1 | up-regulates
|
Endocytosis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260609 |
|
|
Homo sapiens |
|
pmid |
sentence |
19121306 |
However, we did detect WAFL binding to bothWIP and actin by immunoprecipitation (Fig. 4). In conclusion, we propose a model whereby WAFL associates toendocytic vesicles by its coiled-coil domain and is involved in actin-based movement of early endosomes via WIP and binding to actin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
WIPF1 | up-regulates activity
binding
|
WASL |
0.931 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261880 |
|
|
Homo sapiens |
|
pmid |
sentence |
10878810 |
Recruitment of N-WASP to vaccinia is mediated by WASP-interacting protein (WIP), whereas in Shigella WIP is recruited by N-WASP. Our observations show that vaccinia and Shigella activate the Arp2/3 complex to achieve actin-based motility, by mimicking either the SH2/SH3-containing adaptor or Cdc42 signalling pathways to recruit the N-WASP-WIP complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
WIPF1 | up-regulates
|
Early Endosome |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260611 |
|
|
Homo sapiens |
|
pmid |
sentence |
19121306 |
However, we did detect WAFL binding to bothWIP and actin by immunoprecipitation (Fig. 4). In conclusion, we propose a model whereby WAFL associates toendocytic vesicles by its coiled-coil domain and is involved in actin-based movement of early endosomes via WIP and binding to actin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FKBP15 | up-regulates activity
binding
|
WIPF1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260596 |
|
|
Homo sapiens |
|
pmid |
sentence |
19121306 |
However, we did detect WAFL binding to bothWIP and actin by immunoprecipitation (Fig. 4). In conclusion, we propose a model whereby WAFL associates toendocytic vesicles by its coiled-coil domain and is involved in actin-based movement of early endosomes via WIP and binding to actin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |