Dynamic subcellular localization of aquaporin‐7 in white adipocytes. Issue 5 (30th January 2015)

• Record Type: Journal Article
• Authors: Miyauchi, Takayuki; Yamamoto, Hiroyuki; Abe, Yoichiro; Yoshida, Go J.; Rojek, Aleksandra; Sohara, Eisei; Uchida, Shinichi; Nielsen, Søren; Yasui, Masato
• Is Part Of: FEBS letters. Volume 589:Issue 5(2015)
• Page Start: 608
• Page End: 614
• Publication Date: 2015-01-30
• Subjects: LD -- lipid droplet -- ER -- endoplasmic reticulum -- TG -- triacylglycerol -- PKA -- protein kinase A -- CARS -- coherent anti-Stokes Raman scattering -- Lipolysis -- Adipocyte -- Aquaporin-7 -- Comparative gene identification 58; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.01.025
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Aquaporin‐7 (AQP7) is expressed in adipose tissue, permeated by water and glycerol, and is involved in lipid metabolism. AQP7‐null mice develop obesity, insulin resistance, and adipocyte hypertrophy. Here, we show that AQP7 is expressed in adipocyte plasma membranes, and is re‐localized to intracellular membranes in response to catecholamine in mouse white adipose tissue. We found that internalization of AQP7 was induced by PKA activation and comparative gene identification 58 (CGI‐58). This relocation was confirmed by functional studies in 3T3‐L1 adipocytes. Collectively, these results suggest that AQP7 makes several contributions to adipocyte metabolism, in both cortical and intracellular membranes. Abstract : AQP7 is expressed in the adipocyte plasma membrane. AQP7 re‐localizes to inner membranes in response to catecholamine. AQP7 translocation is regulated by CGI‐58 and PKA activation.