Large-scale mass-spectrometric mapping of the yeast kinase/phosphatase interaction (KPI) network; the basis for the SGD ISS annotation transferring a Ser/Thr kinase molecular function to KDX1 from its paralog SLT2. Abstract-only in cache; no KDX1-specific catalytic demonstration is available from the abstract.

Original identification of Mlp1 (KDX1) as an Rlm1-associated protein by yeast two-hybrid; overexpression of MLP1 suppresses the caffeine sensitivity of bck1-delta, and mlp1-delta is additive with mpk1-delta, indicating Rlm1 activity is regulated by both Mpk1 and the "Mlp1 MAP kinase-like kinase".

MLP1/YKL161c is almost undetectable under normal growth but its protein accumulates in large amounts when cell wall integrity is compromised, making the MLP1 promoter an ideal cell-wall-stress reporter.

Mpk1 and its pseudokinase paralog Mlp1 (KDX1) use a noncatalytic mechanism to activate FKS2 transcription; activated (phosphorylated) Mpk1 and Mlp1 were detected in a complex with Swi4 and Swi6 at the FKS2 promoter, conferring DNA-binding ability to Swi4 which then recruits Swi6.

Explicitly describes Mlp1 (KDX1) as "a catalytically inactive paralog of Mpk1"; cell wall stress induction of FKS2/CHA1/YKR013w/YLR042c is only partially dependent on Mlp1 but fully blocked in an mpk1-delta mlp1-delta double mutant, and MLP1 is itself transcriptionally induced by Mpk1 through Rlm1.

Swi4/Swi6 (SBF) activation in response to cell wall stress is noncatalytic and triggered by binding of phosphorylated forms of both Slt2 and the catalytically inactive pseudokinase Mlp1 (KDX1).

The canonical beta3 lysine and DFG aspartate are substituted in Kdx1; the adjacent retained lysine is a different aligned position. Sequence comparison does not itself settle ATP binding or all residual activity.