PUBLICATIONS

Shinde, S.R., Mick, D.U., Aoki, E., Rodrigues, R.B., Gygi, S.P., Nachury, M.V. (2023)

The ancestral ESCRT protein TOM1L2 selects ubiquitinated cargoes for retrieval from cilia. 

Dev Cell, 677-693.e9, doi: 10.1016/j.devcel.2023.03.003

Hansen, J.N., Kaiser, F., Leyendecker, P., Stüven, B., Krause, J.H., Derakhshandeh G., S.F., Jaazba, I., Sroka, T.J., Preval, K.M., Desai, P.B., Kraut, M., Theis, H., Drews, A.D., De-Domenica, E., Händler, K., Pazour, G.J., Mick, D.U., Wachten, D. (2022) 

A cAMP signalosome in primary cilia drives gene expression and kidney cyst formation.

EMBO Rep., 13:e54315, doi: 10.15252/embr.202154315

Wachten, D., Mick, D.U. (2021)

Signal transduction in primary cilia - analyzing and manipulating GPCR and second messenger signaling.

Pharmacol. Ther., 224:107836, doi: 10.1016/j.pharmthera.2021.107836.

May, E.A., Kalocsay, M., Galtier D'Auriac I., Schuster P.S., Gygi SP, Nachury M.V., Mick, D.U. (2021) 

Time-resolved proteomics profiling of the ciliary Hedgehog response.

J. Cell. Biol. 220, e202007207, doi: 10.1083/jcb.202007207

May, E.A., Sroka, T.J., Mick, D.U. (2021)

Phosphorylation and ubiquitylation regulate protein trafficking, signaling, and the biogenesis of primary cilia.

Front. Cell. Dev. Biol. 9, 664279, doi: 10.3389/fcell.2021.664279

Hansen, J-N., Kaiser, F., Klausen, C., Stüven, B., Chong, R., Bönigk, W., Mick, D.U., Möglich, A., Jurisch-Yaksi, N.,  Schmidt, F.I., Wachten, D. (2020)

Nanobody-directed targeting of optogenetic tools to study signaling in the primary cilium.

Elife 9:e57907, doi: 10.7554/eLife.57907

Mick, D.U. (2019)

Establishing cell culture-based experimental setups for proximity labeling using ascorbate peroxidase (APEX).

Methods Mol. Biol. 2008, 29-39. doi: 10.1007/978-1-4939-9537-0_3

Nachury, M.V. and Mick, D.U. (2019)

Establishing and regulating the composition of cilia for signal transduction.

Nat. Rev. Mol. Cell Biol. 20, 389-405. doi: 10.1038/s41580-019-0116-4

Bareth, B., Nikolov, M., Lorenzi, I., Hildenbeutel, M., Mick, D. U., Helbig, C., Urlaub, H., Ott, M., Rehling, P. and Dennerlein, S. (2016)

Oms1 associates with cytochrome c oxidase assembly intermediates to stabilize newly synthesized Cox1.

Mol. Cell. Biol. 27, 1570-1580. doi: 10.1091/mbc.E15-12-0811 

Mick, D. U., Rodrigues, R. B., Leib, R. D., Adams, C. M., Chien, A. S., Gygi, S. P., and Nachury, M. V. (2015)

Proteomics of Primary Cilia by Proximity Labeling.

Dev. Cell 35, 497-512. doi: 10.1016/j.devcel.2015.10.015 

Commented by Nikonova, A. S. and Golemis, E. A. in the same issue

Bareth, B., Dennerlein, S., Mick, D. U., Nikolov, M., Urlaub, H. and Rehling, P. (2013)

The heme a synthase Cox15 associates with cytochrome c oxidase assembly intermediates during Cox1 maturation.

Mol. Cell. Biol., 33, 4128-4137. doi: 10.1128/MCB.00747-13 

Mick, D. U.*, Dennerlein, S.*, Wiese, H., Reinhold, R., Pacheu-Grau, D., Lorenzi, I., Sasarman, F., Weraarpachai, W., Shoubridge, E. A., Warscheid, B. and Rehling, P. (2012)

MITRAC links mitochondrial protein translocation to respiratory chain assembly and translational regulation.

Cell 151, 1528-1541. doi: 10.1016/j.cell.2012.11.053

*authors contributed equally to this work

Reinhold, R., Bareth, B., Balleininger, M., Wissel, M., Rehling, P. and Mick, D. U. (2011)

Mimicking a SURF1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast.

Hum. Mol. Genet. 20, 2379-2393. doi: 10.1093/hmg/ddr145

Lupo, D., Vollmer, C., Deckers, M., Mick, D. U., Tews, I., Sinning, I. and Rehling, P. (2011)

Mdm38 is a 14-3-3-like receptor and associates with the protein synthesis machinery at the inner mitochondrial membrane.

Traffic 12, 1457-1466. doi: 10.1111/j.1600-0854.2011.01239.x 

Mick, D. U., Fox, T. D. and Rehling, P. (2011)

Inventory control: cytochrome c oxidase assembly regulates mitochondrial translation.

Nat. Rev. Mol. Cell Biol. 12, 14-20. doi: 10.1038/nrm3029

Mick, D. U., Vukotic, M., Piechura, H., Meyer, H. E., Warscheid, B., Deckers, M. and Rehling, P. (2010)

Coa3 and Cox14 are essential for negative feedback regulation of COX1 translation in mitochondria.

J. Cell Biol. 191, 141-154. doi: 10.1083/jcb.201007026

Chacinska, A., van der Laan, M., Mehnert, C. S., Guiard, B., Mick, D. U., Hutu, D. P., Truscott, K. N., Wiedemann, N., Meisinger, C., Pfanner, N., and Rehling, P. (2010)

Distinct forms of mitochondrial TOM-TIM supercomplexes define signal-dependent states of preprotein sorting.

Mol. Cell. Biol. 30, 307-318. doi: 10.1128/MCB.00749-09

Bauerschmitt, H.*, Mick, D. U.*, Deckers, M., Vollmer C., Funes S., Kehrein K., Ott M., Rehling P. and Herrmann, J. M. (2010)

Ribosome-binding proteins Mdm38 and Mba1 display overlapping functions for regulation of mitochondrial translation.

Mol. Cell. Biol. 21, 1937-1944. doi: 10.1091/mbc.e10-02-0101

*authors contributed equally to this work

Wagner, K., Mick, D. U., and Rehling, P. (2009)

Protein transport machineries for precursor translocation across the inner mitochondrial membrane.

Biochim. Biophys. Acta 1793, 52-59. doi: 10.1016/j.bbamcr.2008.05.026

Mick, D. U., Wagner, K., van der Laan, M., Frazier, A. E., Perschil, I., Pawlas, M., Meyer, H. E., Warscheid, B., and Rehling, P. (2007)

Shy1 couples Cox1 translational regulation to cytochrome c oxidase assembly.

EMBO J. 26, 4347-4358. doi: 10.1038/sj.emboj.7601862

Meinecke, M., Wagner, R., Kovermann, P., Guiard, B., Mick, D. U., Hutu, D. P., Voos, W., Truscott, K. N., Chacinska, A., Pfanner, N., Rehling, P. (2006)

Tim50 maintains the permeability barrier of the mitochondrial inner membrane.

Science 312, 1523-1526. doi: 10.1126/science.1127628 

Frazier, A. E., Taylor, R. D., Mick, D. U., Warscheid, B., Stoepel, N., Meyer, H. E., Ryan, M. T., Guiard, B., and Rehling, P. (2006)

Mdm38 interacts with ribosomes and is a component of the mitochondrial protein export machinery.

J. Cell Biol. 172, 553-564. doi: 10.1083/jcb.200505060 

Van der Laan, M., Wiedemann, N., Mick, D. U., Guiard, B., Rehling, P, Pfanner, N. (2006)

A role for Tim21 in membrane potential-dependent preprotein sorting in mitochondria.

Curr. Biol. 16, 2271-2276. doi: 10.1016/j.cub.2006.10.025