Vladimir Rogov

Vladimir Rogov

SGC Frankfurt

Rogov

Vladimir Rogov

+49 (0)69 798-29622

Affiliations

Biography

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.

2024

Critical assessment of LC3/GABARAP ligands used for degrader development and ligandability of LC3/GABARAP binding pockets.

Schwalm MP, Dopfer J, Kumar A, Greco FA, Bauer N, Löhr F, Heering J, Cano-Franco S, Lechner S, Hanke T, Jaser I, Morasch V, Lenz C, Fearon D, Marples PG, Tomlinson CWE, Brunello L, Saxena K, Adams NBP, von Delft F, Müller S, Stolz A, Proschak E, Kuster B, Knapp S, Rogov VV

Nat Commun. 2024-11-26 . 15(1):10204 .doi: 10.1038/s41467-024-54409-5

PMID: 39587067

Thermodynamic Characterization of LC3/GABARAP:Ligand Interactions by Isothermal Titration Calorimetry.

Dopfer J, Schwalm MP, Knapp S, Rogov VV

Methods Mol Biol. 2024-8-8 . 2845:219-235 .doi: 10.1007/978-1-0716-4067-8_18

PMID: 39115670

High-Throughput Screening for LC3/GABARAP Binders Utilizing the Fluorescence Polarization Assay.

Schwalm MP, Dopfer J, Knapp S, Rogov VV

Methods Mol Biol. 2024-8-8 . 2845:203-218 .doi: 10.1007/978-1-0716-4067-8_17

PMID: 39115669

2023

Atg8 family proteins, LIR/AIM motifs and other interaction modes.

Rogov VV, Nezis IP, Tsapras P, Zhang H, Dagdas Y, Noda NN, Nakatogawa H, Wirth M, Mouilleron S, McEwan DG, Behrends C, Deretic V, Elazar Z, Tooze SA, Dikic I, Lamark T, Johansen T

Autophagy Rep. 2023-12-31 . 2(1): .doi: 10.1080/27694127.2023.2188523

PMID: 38214012

An atypical GABARAP binding module drives the pro-autophagic potential of the AML-associated NPM1c variant.

Mende H, Khatri A, Lange C, Poveda-Cuevas SA, Tascher G, Covarrubias-Pinto A, Löhr F, Koschade SE, Dikic I, Münch C, Bremm A, Brunetti L, Brandts CH, Uckelmann H, Dötsch V, Rogov VV, Bhaskara RM, Müller S

Cell Rep. 2023-11-22 . 42(12):113484 .doi: 10.1016/j.celrep.2023.113484

PMID: 37999976

The PB1 and the ZZ domain of the autophagy receptor p62/SQSTM1 regulate the interaction of p62/SQSTM1 with the autophagosome protein LC3B.

Alcober-Boquet L, Zang T, Pietsch L, Suess E, Hartmann M, Proschak E, Gross LZF, Sacerdoti M, Zeuzem S, Rogov VV, Leroux AE, Piiper A, Biondi RM

Protein Sci. 2023-11-20 . e4840 .doi: 10.1002/pro.4840

PMID: 37984441

Toward effective Atg8-based ATTECs: Approaches and perspectives.

Schwalm MP, Knapp S, Rogov VV

J Cell Biochem. 2023-2-13 . .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. 2022-7-12 . 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. 2022-6-21 . 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. 2021-7-9 . 22(14): .doi: 10.3390/ijms22147390

PMID: 34299007