Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 29, Issue 17, Pages 2045-2054Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E18-05-0282
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Funding
- National Institutes of Health National Institute of General Medical Sciences [R01 GM067761, R01GM124348-01, 1R01GM097194]
- National Science Foundation Graduate Research Fellowship [DGE1144152]
- Department of Defense through the National Defense Science & Engineering Graduate Fellowship (NDSEG)
- German Research Foundation (DFG) [AR1164/1-1, GRK 1459]
- German Academic Scholarship Foundation
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Rab GTPases recruit peripheral membrane proteins and can define organelle identity. Rab18 localizes to the endoplasmic reticulum (ER) but also to lipid droplets (LDs), where it has been implicated in effector protein recruitment and in defining LD identity. Here, we studied Rab18 localization and function in a human mammary carcinoma cell line. Rab18 localized to the ER and to LD membranes on LD induction, with the latter depending on the Rab18 activation state. In cells lacking Rab18, LDs were modestly reduced in size and numbers, but we found little evidence for Rab18 function in LD formation, LD turnover on cell starvation, or the targeting of several proteins to LDs. We conclude that Rab18 is not a general, necessary component of the protein machinery involved in LD biogenesis or turnover.
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