Purification of Functional Human TRP Channels Recombinantly Produced in Yeast

TY - JOUR

T1 - Purification of Functional Human TRP Channels Recombinantly Produced in Yeast

AU - Zhang, Liying

AU - Wang, Kaituo

AU - Klaerke, Dan Arne

AU - Calloe, Kirstine

AU - Lowrey, Lillian

AU - Pedersen, Per Amstrup

AU - Gourdon, Pontus

AU - Gotfryd, Kamil

PY - 2019/2

Y1 - 2019/2

N2 - (1) Background: Human transient receptor potential (TRP) channels constitute a large family of ion-conducting membrane proteins that allow the sensation of environmental cues. As the dysfunction of TRP channels contributes to the pathogenesis of many widespread diseases, including cardiac disorders, these proteins also represent important pharmacological targets. TRP channels are typically produced using expensive and laborious mammalian or insect cell-based systems. (2) Methods: We demonstrate an alternative platform exploiting the yeast Saccharomyces cerevisiae capable of delivering high yields of functional human TRP channels. We produce 11 full-length human TRP members originating from four different subfamilies, purify a selected subset of these to a high homogeneity and confirm retained functionality using TRPM8 as a model target. (3) Results: Our findings demonstrate the potential of the described production system for future functional, structural and pharmacological studies of human TRP channels.

AB - (1) Background: Human transient receptor potential (TRP) channels constitute a large family of ion-conducting membrane proteins that allow the sensation of environmental cues. As the dysfunction of TRP channels contributes to the pathogenesis of many widespread diseases, including cardiac disorders, these proteins also represent important pharmacological targets. TRP channels are typically produced using expensive and laborious mammalian or insect cell-based systems. (2) Methods: We demonstrate an alternative platform exploiting the yeast Saccharomyces cerevisiae capable of delivering high yields of functional human TRP channels. We produce 11 full-length human TRP members originating from four different subfamilies, purify a selected subset of these to a high homogeneity and confirm retained functionality using TRPM8 as a model target. (3) Results: Our findings demonstrate the potential of the described production system for future functional, structural and pharmacological studies of human TRP channels.

U2 - 10.3390/cells8020148

DO - 10.3390/cells8020148

M3 - Journal article

C2 - 30754715

SN - 2073-4409

VL - 8

SP - 1

EP - 20

JO - Cells

JF - Cells

IS - 2

M1 - 148

ER -