Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R.

Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R. Research Abstract Details 

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Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R. Abstract Text:

Xianhua Yi,Richard Bouley,Herbert Y Lin,Shaliha Bechoua,Tian-Xiao Sun,Elisabetta Del Re,Toshi Shioda,Malay K Raychowdhury,Hua A J Lu,Abdul B Abou-Samra,Dennis Brown,Dennis A Ausiello,

The vasopressin type 2 receptor (V2R) is a G protein-coupled receptor that plays a central role in renal water reabsorption. Termination of ligand (vasopressin) stimulation is an important physiological regulatory event, but few proteins that interact with the V2R during downregulation after vasopressin (VP) binding have been identified. Using yeast two-hybrid screening of a human kidney cDNA library, we show that a 100-kDa protein called ALG-2-interacting protein X (Alix) interacts with the last 29 amino acids of the V2R COOH terminus. This was confirmed by pull-down assays using a GST-V2R-COOH-tail fusion protein. Alix was immunolocalized in principal cells of the kidney, which also express the V2R. The function of the Alix-V2R interaction was studied by transfecting Alix into LLC-PK(1) epithelial cells expressing V2R-green fluorescent protein (GFP). Under basal conditions, V2R-GFP localized mainly at the plasma membrane. On VP treatment, V2R-GFP was internalized into perinuclear vesicles in the nontransfected cells. In contrast, V2R-GFP fluorescence was virtually undetectable 2 h after exposure to VP in cells that coexpressed Alix. Western blotting using an anti-GFP antibody showed marked degradation of the V2R after 2 h in the presence of VP and Alix, a time point at which little or no degradation was detected in the absence of Alix. In contrast, little or no degradation of the parathyroid hormone receptor was detectable in the presence or absence of Alix and/or the PTH ligand. The VP-induced disappearance of V2R-GFP was abolished by chloroquine, a lysosomal degradation inhibitor, but not by MG132, a proteosome inhibitor. These data suggest that Alix increases the rate of lysosomal degradation of V2R and may play an important regulatory role in the VP response by modulating V2R downregulation.

Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R. Publishing Authors By Initials

X Yi,R Bouley,HY Lin,S Bechoua,TX Sun,E Del Re,T Shioda,MK Raychowdhury,HA Lu,AB Abou-Samra,D Brown,DA Ausiello,

For similar fungi: yeasts research abstracts see: fungi: yeasts research

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Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: American journal of physiology. Renal physiology

VOLUME: 292

Page Numbers: F1303-13

Journal Abbreviation:

ISSN: 0363-6127

DAY: 6

MONTH: 02

YEAR: 2007

Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R. Information

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LANGUAGE: eng

NlmUniqueID: 100901990

Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R. Keywords Mesh Terms:

KEYWORDS: Yeasts

MESH TERMS: metabolism

Chemical & Substance for Abstract: Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R. Information

Substance Name: Glutathione Transferase

Registry Number: EC 2.5.1.18

Grant and Affiliation Information for Alix (AIP1) is a vasopressin receptor (V2R)-interacting protein that increases lysosomal degradation of the V2R.

AFFILIATION: Cellular Biophysics Laboratory, Department of Anatomy and Physiology, Kansas State University, Manhattan, Kansas, USA.

Country: United States

AGENCY: United States NIDDK

GRANT: K8-DK-075940-01

ACRONYM: DK

MEDLINETA: Am J Physiol Renal Physiol

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