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Article

Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3

by
Mihaela Matovina
1,*,
Ana Tomašić Paić
1,
Sanja Tomić
1,
Hrvoje Brkić
2,
Lucija Horvat
3,
Lea Barbarić
1,
Vedrana Filić
3,
Marija Pinterić
4,
Snježana Jurić
1 and
Akmaral Kussayeva
1
1
Division of Organic Chemistry and Biochemistry, Ruđer Bošković Institute, Bijenička Cesta 54, 10000 Zagreb, Croatia
2
Faculty of Medicine, Josip Juraj Strossmayer University of Osijek, 31000 Osijek, Croatia
3
Division of Molecular Biology, Ruđer Bošković Institute, Bijenička Cesta 54, 10000 Zagreb, Croatia
4
Division of Molecular Medicine, Ruđer Bošković Institute, Bijenička Cesta 54, 10000 Zagreb, Croatia
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2023, 24(18), 14178; https://doi.org/10.3390/ijms241814178
Submission received: 23 August 2023 / Revised: 11 September 2023 / Accepted: 12 September 2023 / Published: 16 September 2023
(This article belongs to the Special Issue Dipeptidyl Peptidases: From Structure to Function)
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Abstract

Dipeptidyl peptidase 3 (DPP3) is a zinc-dependent exopeptidase with broad specificity for four to eight amino acid residue substrates. It has a role in the regulation of oxidative stress response NRF2–KEAP1 pathway through the interaction with KEAP1. We have conducted stable isotope labeling by amino acids in a cell culture coupled to mass spectrometry (SILAC-MS) interactome analysis of TRex HEK293T cells using DPP3 as bait and identified SH2 Domain-Containing Protein 3C (SH2D3C) as prey. SH2D3C is one of three members of a family of proteins that contain both the SH2 domain and a domain similar to guanine nucleotide exchange factor domains of Ras family GTPases (Ras GEF-like domain), named novel SH2-containing proteins (NSP). NSPs, including SH2D3C (NSP3), are adaptor proteins involved in the regulation of adhesion, migration, tissue organization, and immune response. We have shown that SH2D3C binds to DPP3 through its C-terminal Ras GEF-like domain, detected the colocalization of the proteins in living cells, and confirmed direct interaction in the cytosol and membrane ruffles. Computational analysis also confirmed the binding of the C-terminal domain of SH2D3C to DPP3, but the exact model could not be discerned. This is the first indication that DPP3 and SH2D3C are interacting partners, and further studies to elucidate the physiological significance of this interaction are on the way.
Keywords: protein–protein interaction (PPI); DPP3; SH2D3C protein–protein interaction (PPI); DPP3; SH2D3C

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MDPI and ACS Style

Matovina, M.; Tomašić Paić, A.; Tomić, S.; Brkić, H.; Horvat, L.; Barbarić, L.; Filić, V.; Pinterić, M.; Jurić, S.; Kussayeva, A. Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3. Int. J. Mol. Sci. 2023, 24, 14178. https://doi.org/10.3390/ijms241814178

AMA Style

Matovina M, Tomašić Paić A, Tomić S, Brkić H, Horvat L, Barbarić L, Filić V, Pinterić M, Jurić S, Kussayeva A. Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3. International Journal of Molecular Sciences. 2023; 24(18):14178. https://doi.org/10.3390/ijms241814178

Chicago/Turabian Style

Matovina, Mihaela, Ana Tomašić Paić, Sanja Tomić, Hrvoje Brkić, Lucija Horvat, Lea Barbarić, Vedrana Filić, Marija Pinterić, Snježana Jurić, and Akmaral Kussayeva. 2023. "Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3" International Journal of Molecular Sciences 24, no. 18: 14178. https://doi.org/10.3390/ijms241814178

APA Style

Matovina, M., Tomašić Paić, A., Tomić, S., Brkić, H., Horvat, L., Barbarić, L., Filić, V., Pinterić, M., Jurić, S., & Kussayeva, A. (2023). Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3. International Journal of Molecular Sciences, 24(18), 14178. https://doi.org/10.3390/ijms241814178

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