Author

M. Muqit

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 7

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Assay:proteomics· 6 Organism:human· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

R. Toth· 4 shared A. Knebel· 3 shared H. Ojha· 3 shared A. Shaw· 2 shared A. Waddell· 2 shared O. Antico· 2 shared O. Raimi· 2 shared P. Kakade· 2 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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4 shared papersBiochemistry

R. Toth

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7 papers

Recent·Most cited

Mechanism of human PINK1 activation at the TOM complex in a reconstituted system

O. Raimi, H. Ojha, K. Ehses, V. Dederer, S. Lange, C. P. Rivera, T. Deegan, Y. Chen, M. Wightman, R. Toth, K. Labib, S. Mathea, N. Ranson, R. Fernandez-Busnadiego, M. Muqit

This study identifies TOM20, TOM70, TOM40, and associated subunits as critical for PINK1 activation in a reconstituted yeast system, providing insights for PINK1 activator development.

bioRxiv · Dec 23, 2023Biochemistry

Regulation of Human PINK1 ubiquitin kinase by Serine167, Serine228 and Cysteine412 phosphorylation

A. Waddell, H. Ojha, S. Agarwal, C. Clarke, A. Terriente-Felix, H. Zhou, P. Kakade, A. Knebel, A. Shaw, R. Gourlay, J. Varghese, R. Soares, R. Toth, T. Macartney, P. Eyers, , M. Muqit

This study identifies phosphorylation sites in hPINK1 that regulate its activation and ubiquitin interaction, revealing a novel inhibitory mechanism involving pCys412.

bioRxiv · Mar 31, 2023 · PreprintBiochemistry

Discovery and characterization of non-canonical E2 conjugating enzymes

S. A. Abdul Rehman, E. Di Nisio, C. Cazzaniga, O. Antico, A. Knebel, C. Johnson, F. Lamoliatte, R. Negri, M. Muqit, V. De Cesare

The paper identifies and characterizes non-canonical E2 conjugating enzymes that ubiquitylate serine and threonine instead of lysine, revealing their target substrate and catalytic mechanism.

bioRxiv · Mar 5, 2023 · PreprintBiochemistry

Elaboration of a MALDI-TOF Mass Spectrometry-based Assay of Parkin Activity and High-Throughput screening platform for Parkin Activators

R. Traynor, J. Moran, M. U. Stevens, A. Knebel, B. Behrouz, K. Merchant, C. J. Hastie, P. Davies, M. Muqit, V. De Cesare

The paper develops two MALDI-TOF MS-based methods to quantify Parkin E3 ligase activity in vitro, enabling high-throughput screening of Parkin activators.

bioRxiv · Mar 4, 2022 · PreprintBiochemistry

Mapping of a N-terminal α-helix domain required for human PINK1 stabilisation, Serine228 autophosphorylation and activation in cells

P. Kakade, H. Ojha, O. Raimi, A. Shaw, A. Waddell, J. Ault, S. Burel, K. Brockmann, A. Kumar, M. Ahanger, E. Krysztofinska, T. Macartney, R. Bayliss, J. C. Fitzgerald, M. Muqit

This study identifies an N-terminal α-helix domain in PINK1 critical for its stabilization, autophosphorylation, and activation, linking mutations in this region to Parkinson's disease.

bioRxiv · Sep 6, 2021Biochemistry

Global ubiquitylation analysis of mitochondria in primary neurons identifies physiological Parkin targets following activation of PINK1

O. Antico, A. Ordureau, M. Stevens, F. Singh, M. Gierlinski, E. Barini, M. Rickwood, A. R. Prescott, R. Toth, I. Ganley, W. Harper, M. Muqit

The paper identifies 49 PINK1-dependent ubiquitylated proteins in mouse neurons and develops a resource to visualize mitochondrial ubiquitin sites.

bioRxiv · Apr 1, 2021Biochemistry

PINK1-dependent phosphorylation of Serine111 within the SF3 motif of Rab GTPases impairs effector interactions and LRRK2 mediated phosphorylation at Threonine72

S. Vieweg, K. Mulholland, B. Braeuning, N. Kachariya, Y.-C. Lai, R. Toth, M. Sattler, M. Groll, A. Itzen, M. Muqit

This study shows that PINK1 phosphorylates Rab GTPases at Ser111, which inhibits LRRK2-mediated phosphorylation at Thr72, suggesting PINK1 activators could treat LRRK2-related Parkinson's.

bioRxiv · Sep 12, 2019Biochemistry