Pannexin: Difference between revisions

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== Function ==
== Function ==


'''Pannexin''' (PNX) is a family of single membrane channel-forming glycoprotein.  The family is comprised of 3 members.  PNX1 is expressed in mammalian tissue and plays a role in releasing signals for apoptotic cell clearance. In addition, PNX1 plays a role in propagation of calcium waves, regulation of vascular tone, mucociliary lung clearance, taste-bud function<ref>PMID:22305965</ref>.  PNX1 mediates release of ATP which acts as a signal recruiting macrophages to apoptotic cells.  PNX1 activation requires cleavage of its C-terminal tail by caspase<ref>PMID:22311983</ref>.  
'''Pannexin''' (PNX) is a family of single membrane channel-forming glycoprotein.  The family is comprised of 3 members.  PNX1 is expressed in mammalian tissue and plays a role in releasing signals for apoptotic cell clearance. In addition, PNX1 plays a role in propagation of calcium waves, regulation of vascular tone, mucociliary lung clearance, taste-bud function<ref>PMID:22305965</ref>.  PNX1 mediates release of ATP which acts as a signal recruiting macrophages to apoptotic cells.  PNX1 activation requires cleavage of its C-terminal tail by caspase<ref>PMID:22311983</ref>.  


== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==


The 3D structure of human <scene name='91/916893/Cv/3'>PNX1 shows the pore to constitute 7 subunits</scene>. The C-terminal of PNX1 is cleaved by caspase to produce an active PNX1. The pore transmembrane domains are occupied by lipid molecules which interact with hydrophobic sidechains<ref>PMID:35133866</ref>.  
The 3D structure of human <scene name='91/916893/Cv/3'>PNX1 shows the pore to constitute 7 subunits</scene>. The C-terminal of PNX1 is cleaved by caspase to produce an active PNX1. The pore transmembrane domains are occupied by <scene name='91/916893/Cv/4'>lipid molecules</scene> which interact with hydrophobic sidechains<ref>PMID:35133866</ref>.