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Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains.

Abstract：

: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 regulate distant domains are not well understood. Here we use optical tweezers and molecular dynamics to dissect changes in folding energy landscape associated with cAMP-binding signals transduced between the two CNB domains of protein kinase A (PKA). We find that the response of the energy landscape upon cAMP binding is domain specific, resulting in unique but mutually coordinated tasks: one CNB domain initiates cAMP binding and cooperativity, whereas the other triggers inter-domain interactions that promote the active conformation. Inter-domain interactions occur in a stepwise manner, beginning in intermediate-liganded states between apo and cAMP-bound domains. Moreover, we identify a cAMP-responsive switch, the N3A motif, whose conformation and stability depend on cAMP occupancy. This switch serves as a signaling hub, amplifying cAMP-binding signals during PKA activation.

journal_name

Nat Commun

journal_title

Nature communications

authors

Hao Y,England JP,Bellucci L,Paci E,Hodges HC,Taylor SS,Maillard RA

doi

10.1038/s41467-019-11930-2

subject

Has Abstract

pub_date

2019-09-04 00:00:00

pages

3984

issue

1

issn

2041-1723

pii

10.1038/s41467-019-11930-2

journal_volume

10

pub_type

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