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Cited by 317

The DOI matches its Crossref record; 118 of the 118 references it cites were found in a registry or an index.

Targeting Fat: Mechanisms of Protein Localization to Lipid Droplets

Open access
Kory, Nora, Farese, Robert V., Walther, Tobias C.·2016·Trends in Cell Biology

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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Metadata

Authors
Kory, N., Farese, R. V., & Walther, T. C.
Venue
Trends in Cell Biology
Publisher
Elsevier BV
Published
2016-07
Volume
26
Issue
7
Pages
535-546
ISSN
0962-8924 (ISSN-L)
OpenAlex
W2297029819
Cited by
317
References
118
FWCI
3.45
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Targeting Fat: Mechanisms of Protein Localization to Lipid Droplets. https://app.cochat.ai/papers/10.1016/j.tcb.2016.02.007
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Kory, N., Farese, R. V., & Walther, T. C. (2016). Targeting Fat: Mechanisms of Protein Localization to Lipid Droplets. Trends in Cell Biology. https://doi.org/10.1016/j.tcb.2016.02.007

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.