TY - JOUR
T1 - Ion and solute transport by Prestin in Drosophila and Anopheles
AU - Hirata, Taku
AU - Czapar, Anna
AU - Brin, Lauren
AU - Haritonova, Alyona
AU - Bondeson, Daniel P.
AU - Linser, Paul
AU - Cabrero, Pablo
AU - Thompson, James
AU - Dow, Julian A.T.
AU - Romero, Michael F.
N1 - Funding Information:
This work was supported by NIH : AI45098 (PJL) , DK60845 , EY017732 (MFR) and P50-DK083007 (to JC Lieske; MFR, TH). We thank Heather L. Holmes, Elyse M. Scileppi for excellent technical support as well as Dr. Zara M. Josephs and Dr. Min-Hwang Chang for initial cloning of non-prestin Slc26 Drosophila and Anopheles cDNAs.
PY - 2012/4
Y1 - 2012/4
N2 - The gut and Malpighian tubules of insects are the primary sites of active solute and water transport for controlling hemolymph and urine composition, pH, and osmolarity. These processes depend on ATPase (pumps), channels and solute carriers (Slc proteins). Maturation of genomic databases enables us to identify the putative molecular players for these processes. Anion transporters of the Slc4 family, AE1 and NDAE1, have been reported as HCO3- transporters, but are only part of the story. Here we report Dipteran (Drosophila melanogaster (d) and Anopheles gambiae (Ag)) anion exchangers, belonging to the Slc26 family, which are multi-functional anion exchangers. One Drosophila and two Ag homologues of mammalian Slc26a5 (Prestin) and Slc26a6 (aka, PAT1, CFEX) were identified and designated dPrestin, AgPrestinA and AgPrestinB. dPrestin and AgPrestinB show electrogenic anion exchange (Cl -/nHCO3-, Cl-/SO42- and Cl -/oxalate 2-) in an oocyte expression system. Since these transporters are the only Dipteran Slc26 proteins whose transport is similar to mammalian Slc26a6, we submit that Dipteran Prestin are functional and even molecular orthologues of mammalian Slc26a6. OSR1 kinase increases dPrestin ion transport, implying another set of physiological processes controlled by WNK/SPAK signaling in epithelia. All of these mRNAs are highly expressed in the gut and Malpighian tubules. Dipteran Prestin proteins appear suited for central roles in bicarbonate, sulfate and oxalate metabolism including generating the high pH conditions measured in the Dipteran midgut lumen. Finally, we present and discuss Drosophila genetic models that integrate these processes.
AB - The gut and Malpighian tubules of insects are the primary sites of active solute and water transport for controlling hemolymph and urine composition, pH, and osmolarity. These processes depend on ATPase (pumps), channels and solute carriers (Slc proteins). Maturation of genomic databases enables us to identify the putative molecular players for these processes. Anion transporters of the Slc4 family, AE1 and NDAE1, have been reported as HCO3- transporters, but are only part of the story. Here we report Dipteran (Drosophila melanogaster (d) and Anopheles gambiae (Ag)) anion exchangers, belonging to the Slc26 family, which are multi-functional anion exchangers. One Drosophila and two Ag homologues of mammalian Slc26a5 (Prestin) and Slc26a6 (aka, PAT1, CFEX) were identified and designated dPrestin, AgPrestinA and AgPrestinB. dPrestin and AgPrestinB show electrogenic anion exchange (Cl -/nHCO3-, Cl-/SO42- and Cl -/oxalate 2-) in an oocyte expression system. Since these transporters are the only Dipteran Slc26 proteins whose transport is similar to mammalian Slc26a6, we submit that Dipteran Prestin are functional and even molecular orthologues of mammalian Slc26a6. OSR1 kinase increases dPrestin ion transport, implying another set of physiological processes controlled by WNK/SPAK signaling in epithelia. All of these mRNAs are highly expressed in the gut and Malpighian tubules. Dipteran Prestin proteins appear suited for central roles in bicarbonate, sulfate and oxalate metabolism including generating the high pH conditions measured in the Dipteran midgut lumen. Finally, we present and discuss Drosophila genetic models that integrate these processes.
KW - Cl transport
KW - Gut
KW - Malpighian tubules
KW - Prestin
KW - Slc26
UR - http://www.scopus.com/inward/record.url?scp=84863404367&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84863404367&partnerID=8YFLogxK
U2 - 10.1016/j.jinsphys.2012.01.009
DO - 10.1016/j.jinsphys.2012.01.009
M3 - Article
C2 - 22321763
AN - SCOPUS:84863404367
SN - 0022-1910
VL - 58
SP - 563
EP - 569
JO - Journal of Insect Physiology
JF - Journal of Insect Physiology
IS - 4
ER -