TY - JOUR
T1 - Calcineurin homologous protein
T2 - A multifunctional Ca2+-binding protein family
AU - Di Sole, Francesca
AU - Vadnagara, Komal
AU - Moe, Orson W.
AU - Babich, Victor
PY - 2012
Y1 - 2012
N2 - The calcineurin homologous protein (CHP) belongs to an evolutionarily conserved Ca2+-binding protein subfamily. The CHP subfamily is composed of CHP1, CHP2, and CHP3, which in vertebrates share significant homology at the protein level with each other and between other Ca2+-binding proteins. The CHP structure consists of two globular domains containing from one to four EF-hand structural motifs (calcium-binding regions composed of two helixes, E and F, joined by a loop), the myristoylation, and nuclear export signals. These structural features are essential for the function of the three members of the CHP subfamily. Indeed, CHP1-CHP3 have multiple and diverse essential functions, ranging from the regulation of the plasma membrane Na+/H+ exchanger protein function, to carrier vesicle trafficking and gene transcription. The diverse functions attributed to the CHP subfamily rendered an understanding of its action highly complex and often controversial. This review provides a comprehensive and organized examination of the properties and physiological roles of the CHP subfamily with a view to revealing a link between CHP diverse functions.
AB - The calcineurin homologous protein (CHP) belongs to an evolutionarily conserved Ca2+-binding protein subfamily. The CHP subfamily is composed of CHP1, CHP2, and CHP3, which in vertebrates share significant homology at the protein level with each other and between other Ca2+-binding proteins. The CHP structure consists of two globular domains containing from one to four EF-hand structural motifs (calcium-binding regions composed of two helixes, E and F, joined by a loop), the myristoylation, and nuclear export signals. These structural features are essential for the function of the three members of the CHP subfamily. Indeed, CHP1-CHP3 have multiple and diverse essential functions, ranging from the regulation of the plasma membrane Na+/H+ exchanger protein function, to carrier vesicle trafficking and gene transcription. The diverse functions attributed to the CHP subfamily rendered an understanding of its action highly complex and often controversial. This review provides a comprehensive and organized examination of the properties and physiological roles of the CHP subfamily with a view to revealing a link between CHP diverse functions.
KW - Calcineurin phosphatase
KW - Na/H exchanger
KW - Protein trafficking and cytoskeleton
UR - http://www.scopus.com/inward/record.url?scp=84863919445&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84863919445&partnerID=8YFLogxK
U2 - 10.1152/ajprenal.00628.2011
DO - 10.1152/ajprenal.00628.2011
M3 - Review article
C2 - 22189947
AN - SCOPUS:84863919445
SN - 1931-857X
VL - 303
SP - F165-F179
JO - American Journal of Physiology - Renal Physiology
JF - American Journal of Physiology - Renal Physiology
IS - 2
ER -