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apoptosis in cancer cells
Scientists say they have gained new insight into the role Bax plays in apoptosis.
The Bax protein is known to be a key regulator of apoptosis, mediating the release of cytochrome c to the cytosol via oligomerization in the outer mitochondrial membrane before pore formation.
But the exact mechanism of Bax assembly was previously unclear.
Now, research published in Nature Communications has provided some clarity.
Katia Cosentino, PhD, of the Max Planck Institute for Intelligent Systems in Stuttgart, Germany, and her colleagues conducted this research, examining how the mitochondrial membrane becomes permeable.
The team’s experiments on artificial membrane systems showed that Bax is initially inserted into the membrane as a single molecule.
Once inserted, one Bax molecule will join up with a second Bax molecule to form a stable complex, the Bax dimers. From these dimers, larger complexes are formed.
“Surprisingly, Bax complexes have no standard size, but we observed a mixture of different-sized Bax species, and these species are mostly based on dimer units,” Dr Cosentino said.
She and her colleagues noted that these Bax complexes form the pores through which cytochrome c exits the mitochondrial membrane.
But the process of pore formation is finely controlled by other proteins. Some (such as cBid) enable the assembly of Bax elements, while others (such as Bcl-xL) induce their dismantling.
“The differing size of the Bax complexes in the pore formation is likely part of the reason why earlier investigations on pore formation conveyed contradictory results,” Dr Cosentino said.
She and her colleagues believe that, based on these findings, they can make some initial recommendations for medical intervention in the apoptotic process.
They think that, to promote apoptosis, it should be enough to initiate the first step of activating Bax proteins because the subsequent steps of self-organization will then happen automatically.
Conversely, the team’s findings suggest apoptosis can be prevented when drugs force the dismantling of the Bax dimers into their individual elements. 
apoptosis in cancer cells
Scientists say they have gained new insight into the role Bax plays in apoptosis.
The Bax protein is known to be a key regulator of apoptosis, mediating the release of cytochrome c to the cytosol via oligomerization in the outer mitochondrial membrane before pore formation.
But the exact mechanism of Bax assembly was previously unclear.
Now, research published in Nature Communications has provided some clarity.
Katia Cosentino, PhD, of the Max Planck Institute for Intelligent Systems in Stuttgart, Germany, and her colleagues conducted this research, examining how the mitochondrial membrane becomes permeable.
The team’s experiments on artificial membrane systems showed that Bax is initially inserted into the membrane as a single molecule.
Once inserted, one Bax molecule will join up with a second Bax molecule to form a stable complex, the Bax dimers. From these dimers, larger complexes are formed.
“Surprisingly, Bax complexes have no standard size, but we observed a mixture of different-sized Bax species, and these species are mostly based on dimer units,” Dr Cosentino said.
She and her colleagues noted that these Bax complexes form the pores through which cytochrome c exits the mitochondrial membrane.
But the process of pore formation is finely controlled by other proteins. Some (such as cBid) enable the assembly of Bax elements, while others (such as Bcl-xL) induce their dismantling.
“The differing size of the Bax complexes in the pore formation is likely part of the reason why earlier investigations on pore formation conveyed contradictory results,” Dr Cosentino said.
She and her colleagues believe that, based on these findings, they can make some initial recommendations for medical intervention in the apoptotic process.
They think that, to promote apoptosis, it should be enough to initiate the first step of activating Bax proteins because the subsequent steps of self-organization will then happen automatically.
Conversely, the team’s findings suggest apoptosis can be prevented when drugs force the dismantling of the Bax dimers into their individual elements.
apoptosis in cancer cells
Scientists say they have gained new insight into the role Bax plays in apoptosis.
The Bax protein is known to be a key regulator of apoptosis, mediating the release of cytochrome c to the cytosol via oligomerization in the outer mitochondrial membrane before pore formation.
But the exact mechanism of Bax assembly was previously unclear.
Now, research published in Nature Communications has provided some clarity.
Katia Cosentino, PhD, of the Max Planck Institute for Intelligent Systems in Stuttgart, Germany, and her colleagues conducted this research, examining how the mitochondrial membrane becomes permeable.
The team’s experiments on artificial membrane systems showed that Bax is initially inserted into the membrane as a single molecule.
Once inserted, one Bax molecule will join up with a second Bax molecule to form a stable complex, the Bax dimers. From these dimers, larger complexes are formed.
“Surprisingly, Bax complexes have no standard size, but we observed a mixture of different-sized Bax species, and these species are mostly based on dimer units,” Dr Cosentino said.
She and her colleagues noted that these Bax complexes form the pores through which cytochrome c exits the mitochondrial membrane.
But the process of pore formation is finely controlled by other proteins. Some (such as cBid) enable the assembly of Bax elements, while others (such as Bcl-xL) induce their dismantling.
“The differing size of the Bax complexes in the pore formation is likely part of the reason why earlier investigations on pore formation conveyed contradictory results,” Dr Cosentino said.
She and her colleagues believe that, based on these findings, they can make some initial recommendations for medical intervention in the apoptotic process.
They think that, to promote apoptosis, it should be enough to initiate the first step of activating Bax proteins because the subsequent steps of self-organization will then happen automatically.
Conversely, the team’s findings suggest apoptosis can be prevented when drugs force the dismantling of the Bax dimers into their individual elements.