Joachim Füllekrug

Joachim Füllekrug has a long-standing experience in investigating the function of LD associated proteins, especially FA-metabolizing enzymes and PLINs. His research is focused on the spatial organization of lipid metabolism by LDs and utilizes genetic engineering of immortalized and primary cells followed by biochemical and microscopy analysis.

ORCID: 0000-0001-8511-2164

joachim.fuellekrug[at]med.uni-heidelberg.de

Füllekrug lab

Select Publications

An alternative membrane topology permits lipid droplet localization of peroxisomal fatty acyl-CoA reductase 1
Exner T, Romero-Brey I, Yifrach E, Rivera-Monroy J, Schrul B, Zouboulis CC, Stremmel W, Honsho M, Bartenschlager R, Zalckvar E, Poppelreuther M, Fullekrug J
J Cell Sci 132 2019
doi: 10.1242/jcs.223016 PMID:30745342

The metabolic capacity of lipid droplet localized acyl-CoA synthetase 3 is not sufficient to support local triglyceride synthesis independent of the endoplasmic reticulum in A431 cells
Poppelreuther M, Sander S, Minden F, Dietz MS, Exner T, Du C, Zhang I, Ehehalt F, Knuppel L, Domschke S, Badenhop A, Staudacher S, Ehehalt R, Stremmel W, Thiele C, Heilemann M, Fullekrug J
Biochim Biophys Acta Mol Cell Biol Lipids 1863, 614 2018
doi: 10.1016/j.bbalip.2018.03.003 PMID: 29526665

ACSL4 dictates ferroptosis sensitivity by shaping cellular lipid composition
Doll S, Proneth B, Tyurina YY, Panzilius E, Kobayashi S, Ingold I, Irmler M, Beckers J, Aichler M, Walch A, Prokisch H, Trumbach D, Mao G, Qu F, Bayir H, Fullekrug J, Scheel CH, Wurst W, Schick JA, Kagan VE, Angeli JP, Conrad M
Nat Chem Biol 13, 91 2017
doi: 10.1038/nchembio.2239 PMID: 2784207 PMCID: [PMC5610546] (https://pmc.ncbi.nlm.nih.gov/articles/PMC5610546)

The N-terminal region of acyl-CoA synthetase 3 is essential for both the localization on lipid droplets and the function in fatty acid uptake
Poppelreuther M, Rudolph B, Du C, Grossmann R, Becker M, Thiele C, Ehehalt R, Fullekrug J
J Lipid Res 53, 888 2012
doi: 10.1194/jlr.M024562 PMID: [22357706] (https://pubmed.ncbi.nlm.nih.gov/22357706) PMCID: PMC3329388

FATP4 contributes as an enzyme to the basal and insulin-mediated fatty acid uptake of C(2)C(1)(2) muscle cells
Digel M, Staffer S, Ehehalt F, Stremmel W, Ehehalt R, Fullekrug J
Am J Physiol Endocrinol Metab 301, E785 2011
doi: 10.1152/ajpendo.00079.2011 PMID: 21750264

Copper-induced translocation of the Wilson disease protein ATP7B independent of Murr1/COMMD1 and Rab7
Weiss KH, Lozoya JC, Tuma S, Gotthardt D, Reichert J, Ehehalt R, Stremmel W, Fullekrug J
Am J Pathol 173, 1783 2008
doi: 10.2353/ajpath.2008.071134 PMID: 18974300 PMCID: PMC2626389

Cellular uptake of fatty acids driven by the ER-localized acyl-CoA synthetase FATP4
Milger K, Herrmann T, Becker C, Gotthardt D, Zickwolf J, Ehehalt R, Watkins PA, Stremmel W, Fullekrug J
J Cell Sci 119, 4678 2006
doi: 10.1242/jcs.03280 PMID: 17062637 Gp135/podocalyxin and NHERF-2 participate in the formation of a preapical domain during polarization of MDCK cells
Meder D, Shevchenko A, Simons K, Fullekrug J
J Cell Biol 168, 303 2005
doi: 10.1083/jcb.200407072 PMID: 15642748 PMCID: PMC2171597

Generation of single and double knockdowns in polarized epithelial cells by retrovirus-mediated RNA interference
Schuck S, Manninen A, Honsho M, Fullekrug J, Simons K
Proc Natl Acad Sci U S A 101, 4912 2004
doi: 10.1073/pnas.0401285101 PMID: 15051873 PMCID: PMC387348

Localization and recycling of gp27 (hp24gamma3): complex formation with other p24 family members
Fullekrug J, Suganuma T, Tang BL, Hong W, Storrie B, Nilsson T
Mol Biol Cell 10, 1939 1999
doi: 10.1091/mbc.10.6.1939 PMID: 10359607 PMCID: PMC25391

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