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UID:20260806T224209EDT-4368E6dvHs@132.216.98.100
DTSTAMP:20260807T024209Z
DESCRIPTION:Dr. Edgar C. Young\nAssociate Professor\nDepartment of Molecula
 r Biology and Biochemistry\nSimon Fraser University\, Burnaby BC\n \n“Inte
 gration of cAMP-sensing and voltage-sensing in HCN\n'pacemaker' channels”
 \n \nMany proteins have combined separate domains or modules during\nevolu
 tion to create new functions. Hyperpolarization-activated\nCation (HCN) ch
 annels represent an especially complex combination\nof modules — a cAMP-bi
 nding fold and a voltage-sensing\ntransmembrane domain — enabling cAMP-dep
 endent modulation of\nautomatic electrical rhythms in the brain and heart.
  It is\nwell-established that the cAMP-sensing domain of the HCN channel i
 s\nan autoinhibitory element that hinders channel opening when cAMP is\nab
 sent\, and that cAMP binding then relieves this autoinhibition.\nHowever\,
  I will present our recent evidence that\nautoinhibition-relief is insuffi
 cient to explain all the effects of\ncAMP binding on HCN channels. In part
 icular\, the cAMP-sensing\ndomain enables formation of a kinetic trap for 
 activated (open) HCN\nchannels\, hindering the process of channel deactiva
 tion (closing).\nWe find that whereas deletion of the cAMP-sensing domain 
 mimics\nautoinhibition-relief\, it disables open-state kinetic trapping. T
 he\nstrength of open-state trapping does not correlate with\nautoinhibitio
 n-relief\, and therefore trapping relies on a distinct\nadditional cAMP-de
 pendent mechanism. Moreover\, trapping efficacy is\ncontroled cooperativel
 y by the cAMP-sensing and voltage-sensing\ndomain\, demonstrating a remark
 able degree of functional integration\nfor these disparate modules.\nMANDA
 TORY FOR GRADUATE STUDENTS\n
DTSTART:20101115T170000Z
DTEND:20101115T170000Z
LOCATION:McIntyre Medical Building\, CA\, QC\, Montreal\, H3G 1Y6\, 3655 pr
 omenade Sir William Osler
SUMMARY:Biochemistry Seminar - Dr. Edgar C. Young
URL:/channels/event/biochemistry-seminar-dr-edgar-c-yo
 ung-169306
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