An Unconventional Ligand for Scribble PDZ-4 Domain Mediates Its Interaction with Dusp26
PDZ domains are involved in many cellular processes and are key regulators of the cell physiology. A huge number of studies have investigated the binding specificity of PDZ domains to the carboxyl-terminal sequence of target proteins, while the molecular mechanisms that mediate the recognition of in...
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MDPI AG,
2022-02-01T00:00:00Z.
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LEADER | 00000 am a22000003u 4500 | ||
---|---|---|---|
001 | doaj_166ca89d3e2c46aca41eb8b112dba77f | ||
042 | |a dc | ||
100 | 1 | 0 | |a Raffaella Gallo |e author |
700 | 1 | 0 | |a Erika De Sensi |e author |
700 | 1 | 0 | |a Francesca Storino |e author |
700 | 1 | 0 | |a Simona Panni |e author |
245 | 0 | 0 | |a An Unconventional Ligand for Scribble PDZ-4 Domain Mediates Its Interaction with Dusp26 |
260 | |b MDPI AG, |c 2022-02-01T00:00:00Z. | ||
500 | |a 10.3390/biochem2010006 | ||
500 | |a 2673-6411 | ||
520 | |a PDZ domains are involved in many cellular processes and are key regulators of the cell physiology. A huge number of studies have investigated the binding specificity of PDZ domains to the carboxyl-terminal sequence of target proteins, while the molecular mechanisms that mediate the recognition of internal binding regions are largely unexplored. In the present study, we describe a ligand motif located in the catalytic domain of the phosphatase Dusp26 which mediates its binding to the PDZ-4 of Scribble. Site-directed mutagenesis identified a conserved tyrosine residue as relevant for the binding. The interaction with the PDZ domain could help the phosphatase to recruit its specific targets. | ||
546 | |a EN | ||
690 | |a PDZ domain | ||
690 | |a PDZ internal binding motif | ||
690 | |a Dusp26 | ||
690 | |a scribble | ||
690 | |a dual-specificity phosphatase | ||
690 | |a phosphatase | ||
690 | |a Therapeutics. Pharmacology | ||
690 | |a RM1-950 | ||
690 | |a Biochemistry | ||
690 | |a QD415-436 | ||
655 | 7 | |a article |2 local | |
786 | 0 | |n BioChem, Vol 2, Iss 1, Pp 83-92 (2022) | |
787 | 0 | |n https://www.mdpi.com/2673-6411/2/1/6 | |
787 | 0 | |n https://doaj.org/toc/2673-6411 | |
856 | 4 | 1 | |u https://doaj.org/article/166ca89d3e2c46aca41eb8b112dba77f |z Connect to this object online. |