In a paper from 2009,
(J Cell Biol. 2009 Sep 21;186(6):793-803. Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion.DeVay RM, Dominguez-Ramirez L, Lackner LL, Hoppins S, Stahlberg H, Nunnari J.)
DeVay et al. assumed that OPA-1 and CL are linked in the "obtention" of higher molecular weight OPA1 complexes.
I have a situation with certain cells, where I did not find any changes in OPA1 complex organisation even if the CL amount is lower and if the acyl-chain of most of the CL are modified. My interpretation is that there is always enough CL to do the job and that what is important is the polar head of the cardiolipin which interacts with OPA1 to favor their organisation. The acyl chain being modified but do not enter in the the game for this matter.
Any comments? Any other interpretations?
Hi Patrice! We've never tested this, but yeast and vertebrate mitochondrial dynamics systems do not function exactly alike, so it's quite possible that Opa1 behaves differently from Mgm1 with respect to CL. David Chan might know.
Effectively, it did send a mail to David Chan which has published in 2010 a paper where they demonstrate OPA1 disease alleles associated with DOA display
selective defects in several activities, including cardiolipin association, GTP hydrolysis and membrane tubulations in an artificial system. describe by the authors is the very interesting CL liposomes = 45% POPC, 22% POPE, 8% PI, 25% cardiolipin system, which is efficient.
He is certainly the one how can answer the question properly
Thanks again Don, Hi!
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