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10.1073/pnas.0607465103 http://scihub22266oqcxt.onion/10.1073/pnas.0607465103 17079490!1859892!17079490     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2006 ; 103 (46): 17079-86 Nephropedia Template TP {{tp|p=17079490|t=2006. Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels |pdf=|usr=}}{{17079490}} gab.com Text Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=17079490 #FOAvip The prohibitin (PHB)-domain proteins are membrane proteins that regulate a variety of biological activities, including mechanosensation, osmotic homeostasis, and cell signaling, although the mechanism of this regulation is unknown. We have studied two members of this large protein family, MEC-2, which is needed for touch sensitivity in Caenorhabditis elegans, and Podocin, a protein involved in the function of the filtration barrier in the mammalian kidney, and find that both proteins bind cholesterol. This binding requires the PHB domain (including palmitoylation sites within it) and part of the N-terminally adjacent hydrophobic domain that attaches the proteins to the inner leaflet of the plasma membrane. By binding to MEC-2 and Podocin, cholesterol associates with ion-channel complexes to which these proteins bind: DEG/ENaC channels for MEC-2 and TRPC channels for Podocin. Both the MEC-2-dependent activation of mechanosensation and the Podocin-dependent activation of TRPC channels require cholesterol. Thus, MEC-2, Podocin, and probably many other PHB-domain proteins by binding to themselves, cholesterol, and target proteins regulate the formation and function of large protein-cholesterol supercomplexes in the plasma membrane. Twit Text FOAVip Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=17079490 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17079490 #FOAvip English Wikipedia <ref>{{Cite pmid|17079490}}</ref> Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels #MMPMID17079490 Huber TB; Schermer B; Muller RU; Hohne M; Bartram M; Calixto A; Hagmann H; Reinhardt C; Koos F; Kunzelmann K; Shirokova E; Krautwurst D; Harteneck C; Simons M; Pavenstadt H; Kerjaschki D; Thiele C; Walz G; Chalfie M; Benzing T Proc Natl Acad Sci U S A 2006[Nov]; 103 (46): 17079-86 PMID17079490show ga The prohibitin (PHB)-domain proteins are membrane proteins that regulate a variety of biological activities, including mechanosensation, osmotic homeostasis, and cell signaling, although the mechanism of this regulation is unknown. We have studied two members of this large protein family, MEC-2, which is needed for touch sensitivity in Caenorhabditis elegans, and Podocin, a protein involved in the function of the filtration barrier in the mammalian kidney, and find that both proteins bind cholesterol. This binding requires the PHB domain (including palmitoylation sites within it) and part of the N-terminally adjacent hydrophobic domain that attaches the proteins to the inner leaflet of the plasma membrane. By binding to MEC-2 and Podocin, cholesterol associates with ion-channel complexes to which these proteins bind: DEG/ENaC channels for MEC-2 and TRPC channels for Podocin. Both the MEC-2-dependent activation of mechanosensation and the Podocin-dependent activation of TRPC channels require cholesterol. Thus, MEC-2, Podocin, and probably many other PHB-domain proteins by binding to themselves, cholesterol, and target proteins regulate the formation and function of large protein-cholesterol supercomplexes in the plasma membrane. |Amino Acid Sequence[MESH] |Animals[MESH] |Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism[MESH] |Caenorhabditis elegans/genetics/metabolism[MESH] |Cholesterol/*metabolism[MESH] |Humans[MESH] |Intracellular Signaling Peptides and Proteins/chemistry/genetics/*metabolism[MESH] |Ion Channels/*metabolism[MESH] |Membrane Proteins/chemistry/genetics/*metabolism[MESH] |Mice[MESH] |Molecular Sequence Data[MESH] |Prohibitins[MESH] |Protein Binding[MESH] |Sensitivity and Specificity[MESH]Podocin and MEC-2 bind cholesterol to regulate the activity of associa(epmc).pdf DeepDyve Pubget Overpricing