More than a pore: ion channel signaling complexes.
Voltage- and ligand-gated ion channels form the molecular basis of cellular excitability. With >400 members and accounting for ∼1.5% of the human genome, ion channels are some of the most well studied of all proteins in heterologous expression systems. Yet, ion channels often exhibit unexpected properties in vivo because of their interaction with a variety of signaling/scaffolding proteins. Such interactions can influence the function and localization of ion channels, as well as their coupling to intracellular second messengers and pathways, thus increasing the signaling potential of these ion channels in neurons. Moreover, functions have been ascribed to ion channels that are largely independent of their ion-conducting roles. Molecular and functional dissection of the ion channel proteome/interactome has yielded new insights into the composition of ion channel complexes and how their dysregulation leads to human disease.
Departments of Molecular Physiology and Biophysics, Otolaryngology Head-Neck Surgery, and Neurology, University of Iowa, Iowa City, Iowa 52242, amy-lee@uiowa.edu.
Amy
A
Lee
Institute of Physiology, University of Freiburg, Freiburg 79104, Germany.
Bernd
B
Fakler
Departments of Pharmacology and Cellular and Molecular Physiology, Yale University, New Haven, Connecticut 06520, and.
Leonard K
LK
Kaczmarek
Departments of Pharmacology and Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan 48109.
Lori L
LL
Isom
D000818:Animals; D002448:Cell Adhesion / Q000502:physiology; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology; D007473:Ion Channels / Q000502:physiology*; D009474:Neurons / Q000502:physiology; D021122:Protein Subunits / Q000502:physiology; D040901:Proteomics; D015398:Signal Transduction / Q000502:physiology*
D007473:Ion Channels; D021122:Protein Subunits