Vladimir Rogov

Principle Investigator

Frankfurt
+49 (0)69 798-29622

Vladimir Rogov obtained his PhD in thermodynamics of protein folding and protein-protein interactions at the Institute of Protein Research, Pushchino, Russia, in the lab of Peter Privalov (1995). He continued his career as a senior scientist at the same institute and as a visiting researcher at University of Frankfurt, Germany (lab of Heinz Rüterjans, 1997-2004). He joined the lab of Volker Dötsch at the Institute of Biophysical Chemistry in 2004. Since 2010 Vladimir leads a research group studying protein-protein and protein-ligand interactions across autophagy and ubiquitination pathways. His main research interests include the characterization of affinity, specificity and driving forces of interactions between human autophagy modifiers (LC3/GABARAP proteins) and a broad spectrum of LIR-containing proteins/peptides by several biophysical and biochemical methods, as well as structural aspects of these interactions. He is also focused on molecular mechanisms of enhancing/reducing of the interactions affinity and specificity by post-translational modifications.

Publications VRogov

Characterization of a natural variant of human NDP52 and its functional consequences on mitophagy.
Di Rita A, Angelini DF, Maiorino T, Caputo V, Cascella R, Kumar M, Tiberti M, Lambrughi M, Wesch N, Löhr F, Dötsch V, Carinci M, D'Acunzo P, Chiurchiù V, Papaleo E, Rogov VV, Giardina E, Battistini L, Strappazzon F
Cell Death Differ. 2021 . doi: 10.1038/s41418-021-00766-3
PMID: 33723372

Structural and functional analysis of the GABARAP interaction motif (GIM).
Rogov VV, Stolz A, Ravichandran AC, Rios-Szwed DO, Suzuki H, Kniss A, Löhr F, Wakatsuki S, Dötsch V, Dikic I, Dobson RC, McEwan DG.
EMBO Rep. 2017 18(8):1382-1396. doi: 10.15252/embr.201643587
PMID: 28655748

2023

Toward effective Atg8-based ATTECs: Approaches and perspectives.
Schwalm MP, Knapp S, Rogov VV
J Cell Biochem. 13.02.2023 . doi: 10.1002/jcb.30380
PMID: 36780422

2022

Binding adaptation of GS-441524 diversifies macro domains and downregulate SARS-CoV-2 de-MARylation capacity.
Tsika AC, Gallo A, Fourkiotis NK, Argyriou AI, Sreeramulu S, Löhr F, Rogov VV, Richter C, Linhard V, Gande SL, Altincekic N, Krishnathas R, Elamri I, Schwalbe H, Wollenhaupt J, Weiss MS, Spyroulias GA
J Mol Biol. 12.07.2022 167720. doi: 10.1016/j.jmb.2022.167720
PMID: 35839840

A Toolbox for the Generation of Chemical Probes for Baculovirus IAP Repeat Containing Proteins.
Schwalm MP, Berger LM, Meuter MN, Vasta JD, Corona CR, Röhm S, Berger BT, Farges F, Beinert SM, Preuss F, Morasch V, Rogov VV, Mathea S, Saxena K, Robers MB, Müller S, Knapp S
Front Cell Dev Biol. 21.06.2022 10:886537. doi: 10.3389/fcell.2022.886537
PMID: 35721509

2021

A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1.
Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV
Int J Mol Sci. 09.07.2021 22(14):. doi: 10.3390/ijms22147390
PMID: 34299007

Characterization of a natural variant of human NDP52 and its functional consequences on mitophagy.
Di Rita A, Angelini DF, Maiorino T, Caputo V, Cascella R, Kumar M, Tiberti M, Lambrughi M, Wesch N, Löhr F, Dötsch V, Carinci M, D'Acunzo P, Chiurchiù V, Papaleo E, Rogov VV, Giardina E, Battistini L, Strappazzon F
Cell Death Differ. 15.03.2021 . doi: 10.1038/s41418-021-00766-3
PMID: 33723372

2017

Structural and functional analysis of the GABARAP interaction motif (GIM).
Rogov VV, Stolz A, Ravichandran AC, Rios-Szwed DO, Suzuki H, Kniss A, Löhr F, Wakatsuki S, Dötsch V, Dikic I, Dobson RC, McEwan DG.
EMBO Rep. 01.08.2017 18(8):1382-1396. doi: 10.15252/embr.201643587
PMID: 28655748

Fluorescence-based ATG8 sensors monitor localization and function of LC3/GABARAP proteins.
Stolz A, Putyrski M, Kutle I, Huber J, Wang C, Major V, Sidhu SS, Youle RJ, Rogov VV, Dötsch V, Ernst A, Dikic I.
EMBO J. 15.02.2017 36(4):549-564. doi: 10.15252/embj.201695063
PMID: 28028054

2016

Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation.
Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V.
J Biol Chem. 22.04.2016 291(17):9025-41. doi: 10.1074/jbc.M116.715474
PMID: 26929408

2015

TECPR2 Cooperates with LC3C to Regulate COPII-Dependent ER Export.
Stadel D, Millarte V, Tillmann KD, Huber J, Tamin-Yecheskel BC, Akutsu M, Demishtein A, Ben-Zeev B, Anikster Y, Perez F, Dötsch V, Elazar Z, Rogov V, Farhan H, Behrends C.
Mol Cell. 01.10.2015 60(1):89-104. doi: 10.1016/j.molcel.2015.09.010
PMID: 26431026

CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to spatially restrict TIAM1-RAC1 signaling.
Genau HM, Huber J, Baschieri F, Akutsu M, Dötsch V, Farhan H, Rogov V, Behrends C.
Mol Cell. 19.03.2015 57(6):995-1010. doi: 10.1016/j.molcel.2014.12.040
PMID: 25684205

glqxz9283 sfy39587stf02 mnesdcuix8
sfy39587stf03