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MCL1 — TPT1

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Hprd Interaction: TPT1 — MCL1 (two hybrid) Li et al., J Biol Chem 2001*, Zhang et al., J Biol Chem 2002*
• IRef Hprd Interaction: TPT1 — MCL1 (in vivo) Li et al., J Biol Chem 2001*, Zhang et al., J Biol Chem 2002*
• IRef Hprd Interaction: TPT1 — MCL1 (in vitro) Li et al., J Biol Chem 2001*, Zhang et al., J Biol Chem 2002*

Text-mined interactions from Literome

Zhang et al., J Biol Chem 2002 (Bone Neoplasms...) : Although the depletion of intracellular fortilin by small interfering RNA ( siRNA ) against fortilin ( siRNA-fortilin ) did not affect intracellular MCL1 level, the depletion of intracellular MCL1 by siRNA-MCL1 was associated with the significant reduction of the fortilin protein level, without affecting the fortilin transcript numbers ... Taken together with our previous observation that fortilin overexpression prevents cells from undergoing apoptosis ( Li, F., Zhang, D., and Fujise, K. ( 2001 ) J. Biol. Chem. 276, 47542-47549 ), it is likely that MCL1 , an anti-apoptotic protein inducible by growth and differentiation stimuli, stabilizes another anti-apoptotic protein fortilin maximizing the prosurvival environment in cells
Liu et al., Mol Cell Biol 2005 : While overexpression of TCTP augmented the protein stability of Mcl-1 , knockdown expression of TCTP by RNA interference destabilized Mcl-1 ... Furthermore, TCTP stabilized Mcl-1 through interfering with Mcl-1 's degradation by the ubiquitin dependent proteasome degradation pathway, and the TCTP binding-defective mutant of Mcl-1 ( K257V ) was much more susceptible to degradation and manifested a compromised antiapoptotic activity