Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function . Exists in two forms: the transmembrane, long form , which is tethered to the inner mitochondrial membrane, and the short soluble form , which results from proteolytic cleavage and localizes in the intermembrane space . Both forms cooperate to catalyze the fusion of the mitochondrial inner membrane . The equilibrium between L-OPA1 and S-OPA1 is essential: excess levels of S-OPA1, produced by cleavage by OMA1 following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-OPA1 and S-OPA1, inhibiting mitochondrial fusion . The balance between L-OPA1 and S-OPA1 also influences cristae shape and morphology . Involved in remodeling cristae and the release of cytochrome c during apoptosis . Proteolytic processing by PARL in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C into the mitochondrial intermembrane space . Acts as a regulator of T-helper Th17 cells, which are characterized by cells with fused mitochondria with tight cristae, by mediating mitochondrial membrane remodeling: OPA1 is required for interleukin-17 production . Its role in mitochondrial morphology is required for mitochondrial genome maintenance . ; [Dynamin-like GTPase OPA1, long form]: Constitutes the transmembrane long form that plays a central role in mitochondrial inner membrane fusion and cristae morphology . L-OPA1 and the soluble short form form higher-order helical assemblies that coordinate the fusion of mitochondrial inner membranes . Inner membrane-anchored L-OPA1 molecules initiate membrane remodeling by recruiting soluble S-OPA1 to rapidly polymerize into a flexible cylindrical scaffold encaging the mitochondrial inner membrane . Once at the membrane surface, the formation of S-OPA1 helices induce bilayer curvature . OPA1 dimerization through the paddle region, which inserts into cardiolipin-containing membrane, promotes GTP hydrolysis and the helical assembly of a flexible OPA1 lattice on the membrane, which drives membrane curvature and mitochondrial fusion . Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area . Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions . The equilibrium between L-OPA1 and S-OPA1 influences cristae shape and morphology: increased L-OPA1 levels promote cristae stacking and elongated mitochondria, while increased S-OPA1 levels correlated with irregular cristae packing and round mitochondria shape . ; [Dynamin-like GTPase OPA1, short form]: Constitutes the soluble short form generated by cleavage by OMA1, which plays a central role in mitochondrial inner membrane fusion and cristae morphology . The transmembrane long form and the S-OPA1 form higher-order helical assemblies that coordinate the fusion of mitochondrial inner membranes . Inner membrane-anchored L-OPA1 molecules initiate membrane remodeling by recruiting soluble S-OPA1 to rapidly polymerize into a flexible cylindrical scaffold encaging the mitochondrial inner membrane . Once at the membrane surface, the formation of S-OPA1 helices induce bilayer curvature . OPA1 dimerization through the paddle region, which inserts into cardiolipin-containing membrane, promotes GTP hydrolysis and the helical assembly of a flexible OPA1 lattice on the membrane, which drives membrane curvature and mitochondrial fusion . Excess levels of S-OPA1 produced by cleavage by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-OPA1 and S-OPA1, thereby inhibiting mitochondrial fusion . Involved in mitochondrial safeguard in response to transient mitochondrial membrane depolarization by mediating flickering: cleavage by OMA1 leads to excess production of S-OPA1, preventing mitochondrial hyperfusion . Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area . Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions . The equilibrium between L-OPA1 and S-OPA1 influences cristae shape and morphology: increased L-OPA1 levels promote cristae stacking and elongated mitochondria, while increased S-OPA1 levels correlated with irregular cristae packing and round mitochondria shape . ; [Isoform 1]: Coexpression of isoform 1 with shorter alternative products is required for optimal activity in promoting mitochondrial fusion. ; [Isoform 4]: Isoforms that contain the alternative exon 4b are required for mitochondrial genome maintenance, possibly by anchoring the mitochondrial nucleoids to the inner mitochondrial membrane. ; [Isoform 5]: Isoforms that contain the alternative exon 4b are required for mitochondrial genome maintenance, possibly by anchoring the mitochondrial nucleoids to the inner mitochondrial membrane.

Dynamin-like GTPase OPA1, mitochondrial (EC 3.6.5.5) (Optic atrophy protein 1) [Cleaved into: Dynamin-like GTPase OPA1, long form (L-OPA1); Dynamin-like GTPase OPA1, short form (S-OPA1)]

o60313

Human,Mouse,Rat

WB,IHC

WB 1:1000-1:5000
IHC 1:200-1:500

~112 kD

Rabbit

50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Store at -20°C. Stable for 12 months from date of receipt.