| Title: |
Comparative analysis of PDZ‐binding motifs in the diacylglycerol kinase family. |
| Authors: |
Zambo, Boglarka; Gogl, Gergo; Morlet, Bastien; Eberling, Pascal; Negroni, Luc; Moine, Hervé; Travé, Gilles |
| Source: |
FEBS Journal; Feb2024, Vol. 291 Issue 4, p690-704, 15p |
| Subject Terms: |
Comparative studies; Phosphatidic acids; Mass spectrometry; Kinases; Enzymes |
| Abstract: |
Diacylglycerol kinases (DGKs) control local and temporal amounts of diacylglycerol (DAG) and phosphatidic acid (PA) by converting DAG to PA through phosphorylation in cells. Certain DGK enzymes possess C‐terminal sequences that encode potential PDZ‐binding motifs (PBMs), which could be involved in their recruitment into supramolecular signaling complexes. In this study, we used two different interactomic approaches, quantitative native holdup (nHU) and qualitative affinity purification (AP), both coupled to mass spectrometry (MS) to investigate the PDZ partners associated with the potential PBMs of DGKs. Complementing these results with site‐specific affinity interactomic data measured on isolated PDZ domain fragments and PBM motifs, as well as evolutionary conservation analysis of the PBMs of DGKs, we explored functional differences within different DGK groups. All our results indicate that putative PBM sequences of type II enzymes, namely DGKδ, DGKη, and DGKκ, are likely to be nonfunctional. In contrast, type IV enzymes, namely DGKζ and DGKι, possess highly promiscuous PBMs that interact with a set of PDZ proteins with very similar affinity interactomes. The combination of various interactomic assays and evolutionary analyses provides a useful strategy for identifying functional domains and motifs within diverse enzyme families. [ABSTRACT FROM AUTHOR] |
| : |
Copyright of FEBS Journal is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| Database: |
Complementary Index |