IndraLab

Statements


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reach
"SUMO-1 conjugation is effected via the coordinated collaboration of Mdm2 and the tumour-suppressor ARF, which are both required in a p53, Mdm2, and ARF complex to stimulate p53 SUMOylation via SUMOylation and nucleolar targeting of Mdm2."

sparser
"Three lines of evidence support the genuineness and physiological relevance of ARF-MDM2-p53 nuclear bodies: the dependency of nuclear body formation on the integrity of ARF-MDM2-p53 triprotein interac[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Thus, both the MDM2-binding activity, encoded by the exon 1β, and the nucleolus-localizing activity residing in the exon 2 domain are important for ARF, p53, and MDM2 to form nuclear bodies."

sparser
"ARF binds to the MDM2-P53 complex and prolongs the half-life of P53."

sparser
"In the nucleus, ARF interacts physically and functionally with Mdm2 to inhibit cell cycle progression through activation of p53."

sparser
"Complicated feedback and control mechanisms regulate ARF, Mdm2, and p53 interactions."

sparser
"Formation of a ternary ARFMDM2p53 complex suggests that if ARF regulates MDM2 function, it may not involve simple competitive disruption of MDM2's association with p53."

sparser
"The nuclear bodies formed by p53, MDM2, and ARF, although variable in size, are clearly visible by light microscopy, which suggests that they likely contain a large number of additional proteins and a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Because ARF binding does not compromise the ability of Mdm2 to interact with p53, both binary ARFMdm2 and ternary ARFMdm2p53 complexes can be formed, and their roles in vivo remain a subject of s[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"ARF binds MDM2, preventing it from interacting with p53 [ xref ]."

sparser
"It should be emphasized, however, that overexpression of Mdm2 in some tumors lacking ARF points to more complex biochemical interactions between ARF, Mdm2, and p53 than had been previously expected."

sparser
"Another model proposes that ARF forms a ternary complex with MDM2 and p53 in the nucleoplasm, thereby blocking p53 nuclear export and stabilizing and activating p53 ."

sparser
"ARF-promoted MDM2 degradation is associated with MDM2 modification and concurrent p53 stabilization and accumulation."

sparser
"However, this does not appear to be the case [87,94] , consistent with another similar scenario, such as the protection of p53 by ARF [99] , where Mdm2, p53, and ARF form a complex in which p53 is a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"This model, however, cannot justify the readily observed formation of ARF-MDM2-p53 ternary complex , and how p53 can be stabilized and activated even though still-abundant MDM2 is in the nucleoplasm w[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"ARF binds MDM2 (murine double minute 2) and releases p53 from inhibition by MDM2, resulting in stabilization, accumulation and activation of p53."

sparser
"The observation that ARF binds to a C-terminal domain of MDM2 prompted us to test whether ARF can form a ternary complex with MDM2 and p53."

sparser
"In cells triply transfected with plasmids expressing all three proteins, an ARFMDM2p53 ternary complex was formed as determined by the presence of ARF in anti-p53 immunoprecipitates (lane 18) and re[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"It now appears that p19 ARF binds MDM2 to prevent the degradation of p53 and thus permits p53-induced apoptosis or growth arrest (see Figure 1b ) [31 •• ,32 •• ,33 • ,34 • ] ."

sparser
"Intriguingly, ARF, MDM2, and p53 can form a stable ternary complex, likely bridged by MDM2 via its two separate domains, which can independently interact with p53 and ARF ( Figure 3 )."

sparser
"ARF binds and inhibits MDM2 to activate p53, which has both cell cycle arrest and apoptotic functions."

sparser
"Here, we show that endogenous ARF sequentially interacts with p53 and MDM2 following irradiation of primary human and mouse embryonic fibroblasts."