+ |
PINK1 | down-regulates activity
phosphorylation
|
RAB8A |
0.275 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260268 |
Ser111 |
RNIEEHAsADVEKMI |
in vitro |
|
pmid |
sentence |
31361120 |
For Rab8a, it was shown that serine 111 phosphorylation (pS111) is dependent on the protein kinase PINK1 and that mimicking the phosphorylation at S111 by a serine/glutamate substitution (S111E) impaired Rab8a activation by its cognate nucleotide exchange factor (GEF) Rabin8. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAP3K7 | up-regulates activity
phosphorylation
|
RAB8A |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260266 |
Thr72 |
AGQERFRtITTAYYR |
in vitro |
|
pmid |
sentence |
32227113 |
In a screen for Rab8A kinases we identify TAK1 and MST3 kinases that can efficiently phosphorylate the Switch II residue Threonine72 (Thr72) in a similar manner as LRRK2 in vitro. |Overall our data suggests that the phosphorylation of Rab8A at Ser111 may influence Switch II-binding by regulators, thus disrupting interactions with its cognate GEF and moderately impairs its interaction with GAPs.|The antagonistic interplay between Ser111 phosphorylation and Thr72 phosphorylation is genetically concordant with how respective mutations in PINK1 and LRRK2 cause Parkinson’s disease |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
STK24 | up-regulates activity
phosphorylation
|
RAB8A |
0.279 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260265 |
Thr72 |
AGQERFRtITTAYYR |
in vitro |
|
pmid |
sentence |
32227113 |
In a screen for Rab8A kinases we identify TAK1 and MST3 kinases that can efficiently phosphorylate the Switch II residue Threonine72 (Thr72) in a similar manner as LRRK2 in vitro. |Overall our data suggests that the phosphorylation of Rab8A at Ser111 may influence Switch II-binding by regulators, thus disrupting interactions with its cognate GEF and moderately impairs its interaction with GAPs.|The antagonistic interplay between Ser111 phosphorylation and Thr72 phosphorylation is genetically concordant with how respective mutations in PINK1 and LRRK2 cause Parkinson’s disease |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
LRRK2 | up-regulates activity
phosphorylation
|
RAB8A |
0.337 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260267 |
Thr72 |
AGQERFRtITTAYYR |
in vitro |
|
pmid |
sentence |
32227113 |
In a screen for Rab8A kinases we identify TAK1 and MST3 kinases that can efficiently phosphorylate the Switch II residue Threonine72 (Thr72) in a similar manner as LRRK2 in vitro. |Overall our data suggests that the phosphorylation of Rab8A at Ser111 may influence Switch II-binding by regulators, thus disrupting interactions with its cognate GEF and moderately impairs its interaction with GAPs.|The antagonistic interplay between Ser111 phosphorylation and Thr72 phosphorylation is genetically concordant with how respective mutations in PINK1 and LRRK2 cause Parkinson’s disease |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CEP290 | up-regulates activity
binding
|
RAB8A |
0.732 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252146 |
|
|
Homo sapiens |
|
pmid |
sentence |
18694559 |
CEP290 cooperates with Rab8a to promote ciliogenesis and this function is antagonized by CP110. CEP290 recruits Rab8a to centrosomes. Depletion of CEP290 results in a significant decrease of Rab8a at the centrosome and at the cilium, raising the possibility that CEP290 first recruits Rab8a through direct protein-protein interactions to the centrosome in cycling cells and later promotes ciliogenesis by allowing the entry of Rab8a into the cilium |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BBsome complex | up-regulates activity
binding
|
RAB8A |
0.456 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262562 |
|
|
Homo sapiens |
|
pmid |
sentence |
17574030 |
Interestingly, the BBSome is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPGR | up-regulates activity
guanine nucleotide exchange factor
|
RAB8A |
0.44 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253030 |
|
|
Homo sapiens |
|
pmid |
sentence |
20631154 |
PGR interacts with the small GTPase RAB8A, which participates in cilia biogenesis and maintenance. We show that RPGR primarily associates with the GDP-bound form of RAB8A and stimulates GDP/GTP nucleotide exchange. RPGR functions as a GEF for RAB8A and RPGR–RAB8A association may facilitate ciliary trafficking. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RAB8A | up-regulates
|
Cilium_assembly |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252148 |
|
|
Homo sapiens |
|
pmid |
sentence |
18694559 |
CEP290 cooperates with Rab8a to promote ciliogenesis and this function is antagonized by CP110 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |