Identification of A-Kinase Anchor Protein (AKAP8) as a splicing regulatory factor that impedes EMT and breast cancer metastasis. AKAP8 not only is capable of inhibiting splicing activity of the EMT-promoting splicing regulator hnRNPM through protein-protein interaction it also directly binds to RNA and alters splicing outcomes. Genome-wide analysis shows that AKAP8 promotes an epithelial cell state splicing program.
The results of the present study demonstrate a crucial role for AKAP95 in CYP19A1 expression and oestrogen synthesis in humans luteinized granulosa cells which implies that AKAP95 may be involved in the pathogenesis of polycystic ovary syndrome.
The PKA-binding domain of AKAP8 and the C-terminal domain of DPY30 also called Dpy-30 motif are crucial for the interaction between these proteins. AKAP8 interacts with DPY30 and the RII alpha regulatory subunit of PKA both in the interphase and in mitotic cells. A single amino acid substitution in DPY30 L69D affects its dimerization and completely abolishes its interaction with AKAP8.
Results suggest that ALK generated by alternative transcription Initiation induces chromatin structural changes and heterochromatinization through phosphorylation of AKAP8 in the nucleus.
Using a BioID proximity-based proteomic screen we identify the nuclear pore complex protein TPR as a novel AKAP95 binding partner. We show interaction between AKAP95 and TPR in mitosis and an AKAP95-dependent enrichment of TPR in the spindle microtubule area in metaphase then later in the spindle midzone area.
Ectopic AKAP95 stimulates expression of a chromosomal reporter gene in synergy with MLL1 or MLL2 whereas AKAP95 depletion impairs retinoic acid-mediated gene induction in embryonic stem cells
AMY-1 interacts with S-AKAP84 and this protein in the cytoplasm and the nucleus respectively and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex.
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