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Domain fusion between SNF1‐related kinase subunits during plant evolution
Author(s) -
Lumbreras Victoria,
Albà M Mar,
Kleinow Tatjana,
Koncz Csaba,
Pagès Montserrat
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve001
Subject(s) - arabidopsis , biology , protein subunit , microbiology and biotechnology , protein kinase domain , kinase , regulator , protein kinase a , biochemistry , ampk , function (biology) , cyclin dependent kinase complex , genetics , cyclin dependent kinase 2 , gene , mutant
Members of the conserved SNF1/AMP‐activated protein kinase (AMPK) family regulate cellular responses to environmental and nutritional stress in eukaryotes. Yeast SNF1 and animal AMPKs form a complex with regulatory SNF4/AMPKγ and SIP1/SIP2/GAL83/AMPKβ subunits. The β‐subunits function as target selective adaptors that anchor the catalytic kinase and regulator SNF4/γ‐subunits to their kinase association (KIS) and association with the SNF1 complex (ASC) domains. Here we demonstrate that plant SNF1‐related protein kinases (SnRKs) interact with an adaptor‐regulator protein, AKINβγ, in which an N‐terminal KIS domain characteristic of β‐subunits is fused with a C‐terminal region related to the SNF4/AMPKγ proteins. AKINβγ is constitutively expressed in plants, suppresses the yeast Δ snf4 mutation, and shows glucose‐regulated interaction with the Arabidopsis SnRK, AKIN11. Our results suggest that evolution of AKINβγ reflects a unique function of SNF1‐related protein kinases in plant glucose and stress signalling.