Publications by authors named "Ines Raschke"
Eukaryotic cells respond to signaling molecules with picomolar to nanomolar sensitivities. However, molar concentrations give no suggestion of the sufficient number of molecules per cell and are confusing when referring to physiological situations in which signaling molecules act in an immobilized state. Here, we studied platelet adhesion by thrombin, a key step in normal hemostasis and pathological arterial thrombosis.
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- Mitochondrial fusion is regulated by the protein OPA1, which undergoes cleavage by specific proteases when mitochondria are dysfunctional, leading to fragmentation.
- Two classes of metallopeptidases, m-AAA protease isoenzymes and the OMA1 peptidase, control the cleavage of OPA1 in mitochondria, ensuring a balance between its long and short isoforms essential for fusion.
- Loss of specific proteins like AFG3L2 disrupts the stability of long OPA1 isoforms, causing increased processing by OMA1, which is linked to conditions affecting mitochondrial function and neurodegenerative diseases.
Mitochondria are dynamic organelles, the morphology of which results from an equilibrium between two opposing processes, fusion and fission. Mitochondrial fusion relies on dynamin-related GTPases, the mitofusins (MFN1 and 2) in the outer mitochondrial membrane and OPA1 (optic atrophy 1) in the inner mitochondrial membrane. Apart from a role in the maintenance of mitochondrial DNA, little is known about the physiological role of mitochondrial fusion.
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