The SNF1/AMPK/SnRK1 complex is an intracellular energy sensor composed of three types of subun
its: the SnRK1 kinase and two regulatory, non-catalytic subun
its (designated β and γ). We have previously described an atypical plant γ-subun
it, AKINβγ, which contains an N-terminal tail similar to the so-called KIS domain normally present in β-subun
its. However,
it is not known whether AKINβγ normally associates w
ith endogenous SnRK1 complexes in vivo, nor how
its unique domain structure might contribute to SnRK1 function. Here, we present evidence that maize AKINβγ is an integral component of active SnRK1 complexes in plant cells. Using complementary methodological approaches, we also show that AKINβγ associates through homomeric interactions mediated by both, the γ- and, unexpectedly, the KIS/CBM domain.
Structured summary
MINT-7040005: AKIN (uniprotkb:B4FX20) and AKIN (uniprotkb:B4FX20) physically interact (MI:0914) by chromatography technologies (MI:0091)
MINT-7039992: AKIN (uniprotkb:B4FX20) and AKIN (uniprotkb:B4FX20) physically interact (MI:0915) by bimolecular fluorescence complementation (MI:0809)
MINT-7040024, MINT-7040044, MINT-7040067: AKIN (uniprotkb:B4FX20) and AKIN (uniprotkb:B4FX20) bind (MI:0407) by pull down (MI:0096)
MINT-7039978: SnRK1 (uniprotkb:Q8H1L5) and AKIN (uniprotkb:B4FX20) physically interact (MI:0915) by bimolecular fluorescence complementation (MI:0809)