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      Targeting Fat: Mechanisms of Protein Localization to Lipid Droplets

      research-article
      1 , 1 , 2 , 3 , 1 , 2 , 3 , 4
      Trends in cell biology

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          Abstract

          How proteins specifically localize to the phospholipid monolayer surface of lipid droplets (LDs) is being unraveled. We review here the major known pathways of protein targeting to LDs and suggest a classification framework based on the localization origin for the protein. Class I proteins often have a membrane-embedded, hydrophobic ‘hairpin’ motif, and access LDs from the endoplasmic reticulum (ER) either during LD formation or after formation via ER-LD membrane bridges. Class II proteins access the LD surface from the cytosol and bind through amphipathic helices or other hydrophobic domains. Other proteins require lipid modifications or protein-protein interactions to bind to LDs. We summarize knowledge for targeting and removal of the different classes, and highlight areas needing investigation.

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          Author and article information

          Journal
          9200566
          21041
          Trends Cell Biol
          Trends Cell Biol.
          Trends in cell biology
          0962-8924
          1879-3088
          4 March 2016
          16 March 2016
          July 2016
          01 July 2017
          : 26
          : 7
          : 535-546
          Affiliations
          [1 ]Department of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA, USA
          [2 ]Department of Cell Biology, Harvard Medical School, Boston, MA, USA
          [3 ]Broad Institute of Massachusetts Institute of Technology (MIT) and Harvard, Cambridge, MA, USA
          [4 ]Howard Hughes Medical Institute (HHMI), Boston, MA, USA
          Author notes
          [* ]Correspondence: robert@ 123456hsph.harvard.edu (R.V. Farese Jr) and twalther@ 123456hsph.harvard.edu (T.C. Walther)
          Article
          PMC4976449 PMC4976449 4976449 nihpa764826
          10.1016/j.tcb.2016.02.007
          4976449
          26995697
          da3675a4-925c-44a4-a88c-3f64c5aa679f
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