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AKT phosphorylates RAC1 on S71. 22 / 22
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sparser
"Finally, previous work by our group and others provided evidence that Akt can phosphorylate Rac1 at Ser 71 and that this effect is correlated with reduced Rac1 activation ( xref ; xref )."

sparser
"For example, AKT phosphorylation of serine71 on Rac1 enhances guanine diphosphate binding [ xref ]."

sparser
"Rac1 is phosphorylated on S71 by Akt, leading to inhibition of GTP binding, but not Rac1 GTPase activity [ xref ]."

reach
"Finally, previous work by our group and others provided evidence that Akt can phosphorylate Rac1 at Ser 71 and that this effect is correlated with reduced Rac1 activation."

sparser
"Ser‐71 phosphorylated Rac1/Cdc42 appear to be in their active conformation according to pull‐down assay with PAK CRIB‐domain and Rho‐GDI. xref Both Rac1 and Cdc42 belong to GTPases of the Rho subfamily that exert on the actin cytoskeleton as well as differentiation and function of osteoclast. xref , xref However, evidence showed that the phosphorylation of Rac1 at Ser‐71 by Akt may inhibit GTP binding of Rac1, attenuating the signal transduction pathway downstream of Rac1. xref , xref , xref It is quite possible that the enhanced phosphorylation of Cdc42 can be associated with the augmented osteoclast differentiation in the ADOII patient."

sparser
"It is not clear whether Rac1 is a phosphorylation target for PKA, but Kwon et al. demonstrated phosphorylation of Rac1 on Ser-71 by Akt in human melanoma cells xref ."

reach
"Rac1 can also be phosphorylated by the Akt kinase at Ser 71, which is embedded in the consensus sequence 64 ydRIRplSYp 73."

sparser
"Rac1 enhances tissue invasion of prostate cancer cells by activating Rho GTPases and promoting activation of MMPs [ xref , xref ], and Akt phosphorylates Rac1 at Ser71 to inhibit its GTPase activity [ xref , xref ]."

reach
"Rac1 is phosphorylated on S71 by Akt, leading to inhibition of GTP binding, but not Rac1 GTPase activity [XREF_BIBR]."

No evidence text available

reach
"Rac1 enhances tissue invasion of prostate cancer cells by activating Rho GTPases and promoting activation of MMPs [XREF_BIBR, XREF_BIBR], and Akt phosphorylates Rac1 at Ser71 to inhibit its GTPase activity [XREF_BIBR, XREF_BIBR]."

sparser
"In addition, Rac1 phosphorylation at Ser71 by Akt has been shown to determine downstream effector specificity and degradation, while Y64 phosphorylation by non-receptor tyrosine-kinases (e.g., FAK, Src) regulates targeting to focal adhesions and GEFs ( xref ; xref ; xref ; xref ; xref ; xref )."

sparser
"Rac1 is phosphorylated on S71 by Akt [ xref ] ( xref )."

sparser
"Furthermore, phosphorylation of Rac1 S71 by AKT was shown to facilitate its ubiquitination and subsequent proteasomal degradation of Rac1 [ xref ]."
| PMC

"Akt protein kinase inhibits Rac1-GTP binding through phosphorylation at serine 71 of Rac1"

sparser
"On the other hand, phosphorylation of serine-71 on Rac1 by serine/threonine kinase Akt seems to have different effects – inhibiting the GTP-binding activity of Rac1 with no significant change in GTPase activity [ xref ]."

sparser
"Rac1 can also be phosphorylated by the Akt kinase at Ser-71, which is embedded in the consensus sequence 64 yd R IRpl SY p 73 ."

reach
"16 Akt1 is involved in cellular survival pathways, by inhibiting apoptotic processes and activated Akt can phosphorylate Rac1 at Ser71 reducing Rac1 activation."

"The results suggest that Akt kinase of the phosphoinositide 3-kinase signal transduction pathway phosphorylates serine 71 of Rac1 as one of its authentic substrates and modulates the Rac1 signal transduction pathway through phosphorylation."

reach
"Rac1 is phosphorylated on 71 S by Akt, which does not change Rac1 GTPase activity of Rac1, but inhibits its binding to GTP [XREF_BIBR]."

sparser
"Rac1 is phosphorylated on Ser71 by the serine/threonine kinase protein kinase B (also known as AKT) to inhibit GTP binding [ xref , xref ], similar to the Cdc42 Ser71 phosphorylation."
| PMC

sparser
"AKT serine/threonine kinase phosphorylates Rac1 on Ser71 to decrease its GTP-binding activity [ xref ]."