Negatively‐charged residues in the polar carboxy‐terminal region in FSP27 are indispensable for expanding lipid droplets. Issue 6 (15th March 2016)

• Record Type: Journal Article
• Authors: Tamori, Yoshikazu; Tateya, Sanshiro; Ijuin, Takeshi; Nishimoto, Yuki; Nakajima, Shinsuke; Ogawa, Wataru
• Is Part Of: FEBS letters. Volume 590:Issue 6(2016)
• Page Start: 750
• Page End: 759
• Publication Date: 2016-03-15
• Subjects: adipocyte -- fat specific protein of 27 kDa -- lipid droplet -- lipid droplet enlargement -- negatively‐charged amino acid -- structure and function; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12114
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : FSP27 has an important role in large lipid droplet (LD) formation because it exchanges lipids at the contact site between LDs. In the present study, we clarify that the amino‐terminal domain of FSP27 (amino acids 1–130) is dispensable for LD enlargement, although it accelerates LD growth. LD expansion depends on the carboxy‐terminal domain of FSP27 (amino acids 131–239). Especially, the negative charge of the acidic residues (D215, E218, E219 and E220) in the polar carboxy‐terminal region (amino acids 202–239) is essential for the enlargement of LD. We propose that the carboxy‐terminal domain of FSP27 has a crucial role in LD expansion, whereas the amino‐terminal domain only has a supportive role. Abstract : The amino‐terminal half domain of FSP27 increases the efficacy of LD enlargement. The carboxy‐terminal half domain of FSP27 is indispensable for LD enlargement. The negative charge of the acidic amino acids (D215, E218, E219 and E220) is essential for LD growth.