title: Phosphatidic acid phospholipase A1 mediates ER-Golgi transit of a family of G protein-coupled receptors.
abstract: The coat protein II (COPII)-coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum (ER) to the Golgi complex. Recruitment of cargo into COPII vesicles requires an interaction of COPII proteins either with the cargo molecules directly or with cargo receptors for anterograde trafficking. We show that cytosolic phosphatidic acid phospholipase A1 (PAPLA1) interacts with COPII protein family members and is required for the transport of Rh1 (rhodopsin 1), an N-glycosylated G protein-coupled receptor (GPCR), from the ER to the Golgi complex. In papla1 mutants, in the absence of transport to the Golgi, Rh1 is aberrantly glycosylated and is mislocalized. These defects lead to decreased levels of the protein and decreased sensitivity of the photoreceptors to light. Several GPCRs, including other rhodopsins and Bride of sevenless, are similarly affected. Our findings show that a cytosolic protein is necessary for transit of selective transmembrane receptor cargo by the COPII coat for anterograde trafficking.
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute, Frederick, MD 21702.
authors.forename: Govind
authors.initials: G
authors.lastname: Kunduri
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute, Frederick, MD 21702.
authors.forename: Changqing
authors.initials: C
authors.lastname: Yuan
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute, Frederick, MD 21702.
authors.forename: Velayoudame
authors.initials: V
authors.lastname: Parthibane
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute, Frederick, MD 21702.
authors.forename: Katherine M
authors.initials: KM
authors.lastname: Nyswaner
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute, Frederick, MD 21702.
authors.forename: Ritu
authors.initials: R
authors.lastname: Kanwar
authors.affiliation: Electron Microscopy Laboratory, Frederick National Laboratory for Cancer Research, Frederick, MD 21702.
authors.forename: Kunio
authors.initials: K
authors.lastname: Nagashima
authors.affiliation: Department of Cell and Developmental Biology, University of Colorado, Aurora, CO 80045.
authors.forename: Steven G
authors.initials: SG
authors.lastname: Britt
authors.affiliation: Complex Carbohydrate Research Center, The University of Georgia, Athens, GA 30602.
authors.forename: Nickita
authors.initials: N
authors.lastname: Mehta
authors.affiliation: Complex Carbohydrate Research Center, The University of Georgia, Athens, GA 30602.
authors.forename: Varshika
authors.initials: V
authors.lastname: Kotu
authors.affiliation: Complex Carbohydrate Research Center, The University of Georgia, Athens, GA 30602.
authors.forename: Mindy
authors.initials: M
authors.lastname: Porterfield
authors.affiliation: Complex Carbohydrate Research Center, The University of Georgia, Athens, GA 30602.
authors.forename: Michael
authors.initials: M
authors.lastname: Tiemeyer
authors.affiliation: Department of Biological Sciences, Dartmouth College, Hanover, NH 03755.
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Dolph
authors.affiliation: Program in Gene Function and Expression, University of Massachusetts Medical School, Worcester, MA 01605.
authors.forename: Usha
authors.initials: U
authors.lastname: Acharya
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute, Frederick, MD 21702 acharyaj@mail.nih.gov.
authors.forename: Jairaj K
authors.initials: JK
authors.lastname: Acharya
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D029721:Drosophila Proteins / Q000737:chemistry / Q000502:physiology*; D004331:Drosophila melanogaster / Q000201:enzymology*; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D005260:Female; D006056:Golgi Apparatus / Q000201:enzymology*; D008297:Male; D008969:Molecular Sequence Data; D054466:Phospholipases A1 / Q000737:chemistry / Q000502:physiology*; D021381:Protein Transport; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism*
chemical_list: D029721:Drosophila Proteins; D043562:Receptors, G-Protein-Coupled; C000591841:PAPLA1 protein, Drosophila; D054466:Phospholipases A1