Role for Tyrosine Phosphorylation of A-kinase Anchoring Protein 8 (AKAP8) in Its Dissociation from Chromatin and the Nuclear Matrix.

The Journal of Biological Chemistry
Sho KubotaN Yamaguchi

Abstract

Protein-tyrosine phosphorylation regulates a wide variety of cellular processes at the plasma membrane. Recently, we showed that nuclear tyrosine kinases induce global nuclear structure changes, which we called chromatin structural changes. However, the mechanisms are not fully understood. In this study we identify protein kinase A anchoring protein 8 (AKAP8/AKAP95), which associates with chromatin and the nuclear matrix, as a nuclear tyrosine-phosphorylated protein. Tyrosine phosphorylation of AKAP8 is induced by several tyrosine kinases, such as Src, Fyn, and c-Abl but not Syk. Nucleus-targeted Lyn and c-Src strongly dissociate AKAP8 from chromatin and the nuclear matrix in a kinase activity-dependent manner. The levels of tyrosine phosphorylation of AKAP8 are decreased by substitution of multiple tyrosine residues on AKAP8 into phenylalanine. Importantly, the phenylalanine mutations of AKAP8 inhibit its dissociation from nuclear structures, suggesting that the association/dissociation of AKAP8 with/from nuclear structures is regulated by its tyrosine phosphorylation. Furthermore, the phenylalanine mutations of AKAP8 suppress the levels of nuclear tyrosine kinase-induced chromatin structural changes. In contrast, AKAP8 knockd...Continue Reading

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Citations

Nov 8, 2015·Nucleic Acids Research·Kiran Mahajan, Nupam P Mahajan
Nov 25, 2016·Journal of Cellular Biochemistry·Noritaka YamaguchiNaoto Yamaguchi
Jul 29, 2018·American Journal of Medical Genetics. Part a·Laiara Cristina de SouzaTársis Paiva Vieira
Aug 16, 2018·Annual Review of Cell and Developmental Biology·Christina SchoenherrAdam Byron
Jul 4, 2020·The Journal of Biological Chemistry·Christina SchoenherrMargaret C Frame
Dec 22, 2016·The Journal of Biological Chemistry·Mariko MoriiNaoto Yamaguchi
Dec 19, 2020·Pharmacological Reviews·Manuela ZaccoloMiguel J Lobo
Jan 30, 2021·Scientific Reports·Mariko MoriiNaoto Yamaguchi

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