Cellular Localization and Biochemical Analysis of Mammalian CDC50A, a Glycosylated β-subunit for P4 ATPases

Dineke E. Folmer; Kam S. Mok; Sebastiaan W. de Wee; Suzanne Duijst; Johan K. Hiralall; Jurgen Seppen; Ronald P.J. Oude Elferink; Coen C. Paulusma

doi:https://doi.org/10.1369/0022155411435705

Cellular Localization and Biochemical Analysis of Mammalian CDC50A, a Glycosylated β-subunit for P4 ATPases

Dineke E. Folmer, Kam S. Mok, Sebastiaan W. de Wee, Suzanne Duijst, Johan K. Hiralall, Jurgen Seppen, Ronald P.J. Oude Elferink, Coen C. Paulusma

Research output: Contribution to journal › Article › Academic › peer-review

19 Citations (Scopus)

Abstract

CDC50 proteins are β-subunits for P4 ATPases, which upon heterodimerization form a functional phospholipid translocation complex. Emerging evidence in mouse models and men links mutations in P4 ATPase genes with human disease. This study analyzed the tissue distribution and cellular localization of CDC50A, the most abundant and ubiquitously expressed CDC50 homologue in the mouse. The authors have raised antibodies that detect mouse and human CDC50A and studied CDC50A localization and glycosylation status in mouse liver cells. CDC50A is a terminal-glycosylated glycoprotein and is expressed in hepatocytes and liver sinusoidal endothelial cells, where it resides in detergent-resistant membranes. In pancreas and stomach, CDC50A localized to secretory vesicles, whereas in the kidney, CDC50A localized to the apical region of proximal convoluted tubules of the cortex. In WIF-B9 cells, CDC50A partially costains with the trans-Golgi network. Data suggest that CDC50A is present as a fully glycosylated protein in vivo, which presumes interaction with distinct P4 ATPases.

Original language	English
Pages (from-to)	205-218
Number of pages	14
Journal	Journal of Histochemistry and Cytochemistry
Volume	60
Issue number	3
DOIs	https://doi.org/10.1369/0022155411435705
Publication status	Published - Mar 2012

Keywords

-subunit
CDC50
P4 ATPase
b
cholestasis
membrane
phospholipid
vesicular transport

Access to Document

https://doi.org/10.1369/0022155411435705

Cite this

@article{6f4696c7c4114b87859e2b380b5715b3,

title = "Cellular Localization and Biochemical Analysis of Mammalian CDC50A, a Glycosylated β-subunit for P4 ATPases",

abstract = "CDC50 proteins are β-subunits for P4 ATPases, which upon heterodimerization form a functional phospholipid translocation complex. Emerging evidence in mouse models and men links mutations in P4 ATPase genes with human disease. This study analyzed the tissue distribution and cellular localization of CDC50A, the most abundant and ubiquitously expressed CDC50 homologue in the mouse. The authors have raised antibodies that detect mouse and human CDC50A and studied CDC50A localization and glycosylation status in mouse liver cells. CDC50A is a terminal-glycosylated glycoprotein and is expressed in hepatocytes and liver sinusoidal endothelial cells, where it resides in detergent-resistant membranes. In pancreas and stomach, CDC50A localized to secretory vesicles, whereas in the kidney, CDC50A localized to the apical region of proximal convoluted tubules of the cortex. In WIF-B9 cells, CDC50A partially costains with the trans-Golgi network. Data suggest that CDC50A is present as a fully glycosylated protein in vivo, which presumes interaction with distinct P4 ATPases.",

keywords = "-subunit, CDC50, P4 ATPase, b, cholestasis, membrane, phospholipid, vesicular transport",

author = "Folmer, {Dineke E.} and Mok, {Kam S.} and {de Wee}, {Sebastiaan W.} and Suzanne Duijst and Hiralall, {Johan K.} and Jurgen Seppen and {Oude Elferink}, {Ronald P.J.} and Paulusma, {Coen C.}",

year = "2012",

month = mar,

doi = "https://doi.org/10.1369/0022155411435705",

language = "English",

volume = "60",

pages = "205--218",

journal = "Journal of Histochemistry and Cytochemistry",

issn = "0022-1554",

publisher = "Histochemical Society Inc.",

number = "3",

}

TY - JOUR

T1 - Cellular Localization and Biochemical Analysis of Mammalian CDC50A, a Glycosylated β-subunit for P4 ATPases

AU - Folmer, Dineke E.

AU - Mok, Kam S.

AU - de Wee, Sebastiaan W.

AU - Duijst, Suzanne

AU - Hiralall, Johan K.

AU - Seppen, Jurgen

AU - Oude Elferink, Ronald P.J.

AU - Paulusma, Coen C.

PY - 2012/3

Y1 - 2012/3

N2 - CDC50 proteins are β-subunits for P4 ATPases, which upon heterodimerization form a functional phospholipid translocation complex. Emerging evidence in mouse models and men links mutations in P4 ATPase genes with human disease. This study analyzed the tissue distribution and cellular localization of CDC50A, the most abundant and ubiquitously expressed CDC50 homologue in the mouse. The authors have raised antibodies that detect mouse and human CDC50A and studied CDC50A localization and glycosylation status in mouse liver cells. CDC50A is a terminal-glycosylated glycoprotein and is expressed in hepatocytes and liver sinusoidal endothelial cells, where it resides in detergent-resistant membranes. In pancreas and stomach, CDC50A localized to secretory vesicles, whereas in the kidney, CDC50A localized to the apical region of proximal convoluted tubules of the cortex. In WIF-B9 cells, CDC50A partially costains with the trans-Golgi network. Data suggest that CDC50A is present as a fully glycosylated protein in vivo, which presumes interaction with distinct P4 ATPases.

AB - CDC50 proteins are β-subunits for P4 ATPases, which upon heterodimerization form a functional phospholipid translocation complex. Emerging evidence in mouse models and men links mutations in P4 ATPase genes with human disease. This study analyzed the tissue distribution and cellular localization of CDC50A, the most abundant and ubiquitously expressed CDC50 homologue in the mouse. The authors have raised antibodies that detect mouse and human CDC50A and studied CDC50A localization and glycosylation status in mouse liver cells. CDC50A is a terminal-glycosylated glycoprotein and is expressed in hepatocytes and liver sinusoidal endothelial cells, where it resides in detergent-resistant membranes. In pancreas and stomach, CDC50A localized to secretory vesicles, whereas in the kidney, CDC50A localized to the apical region of proximal convoluted tubules of the cortex. In WIF-B9 cells, CDC50A partially costains with the trans-Golgi network. Data suggest that CDC50A is present as a fully glycosylated protein in vivo, which presumes interaction with distinct P4 ATPases.

KW - -subunit

KW - CDC50

KW - P4 ATPase

KW - b

KW - cholestasis

KW - membrane

KW - phospholipid

KW - vesicular transport

UR - http://www.scopus.com/inward/record.url?scp=84859642842&partnerID=8YFLogxK

U2 - https://doi.org/10.1369/0022155411435705

DO - https://doi.org/10.1369/0022155411435705

M3 - Article

C2 - 22253360

SN - 0022-1554

VL - 60

SP - 205

EP - 218

JO - Journal of Histochemistry and Cytochemistry

JF - Journal of Histochemistry and Cytochemistry

IS - 3

ER -

Cellular Localization and Biochemical Analysis of Mammalian CDC50A, a Glycosylated β-subunit for P4 ATPases

Abstract

Keywords

Access to Document

Other files and links

Cite this