When the J-domain of the heat shock protein DnaJB1 is fused to the catalytic (C) subunit of
cAMP-dependent protein kinase (PKA), replacing exon 1, this fusion protein, JC subunit …

The LINC complex is found in a wide variety of organisms and is formed by the transluminal
interaction between outer-and inner-nuclear-membrane KASH and SUN proteins …

Protein kinase A (PKA) holoenzyme, comprised of a cAMP-binding regulatory (R)-subunit
dimer and 2 catalytic (C)-subunits, is the master switch for cAMP-mediated signaling. Of the …

Phosphorylation is a major regulator of protein interactions; however, the mechanisms by
which regulation occurs are not well understood. Here we identify a salt-bridge competition …

Fibrolamellar hepatocellular carcinoma (FLHCC) is driven by J-PKAcα, a kinase fusion
chimera of the J domain of DnaJB1 with PKAcα, the catalytic subunit of protein kinase A …

Parasitic protozoa of the genus Leishmania cycle between the phagolysosome of
mammalian macrophages, where they reside as rounded intracellular amastigotes, and the …

Cyclic nucleotide-binding (CNB) domains allosterically regulate the activity of proteins with
diverse functions, but the mechanisms that enable the cyclic nucleotide-binding signal to …

Dynamic allostery is a relatively new paradigm where certain external perturbations may
lead to modulation of conformational dynamics at a distant part of a protein without …

The DNAJB1–PRKACA oncogenic gene fusion results in an active kinase enzyme, J-PKAcα,
that has been identified as an attractive antitumor target for fibrolamellar hepatocellular …

Protein kinases are dynamic molecular switches that sample multiple conformational states.
The regulatory subunit of PKA harbors two cAMP-binding domains [cyclic nucleotide-binding …