High impact information on NEK6

• Nercc1 binds to another NIMA-like kinase, Nek6, and also binds specifically to the Ran GTPase through both its catalytic and its RCC1-like domains, preferring RanGDP in vivo [1].
• Nercc1/Nek9 is likely to be responsible for the activation of Nek6 during mitosis and probably participates in the regulation of Nek7 as well [2].
• In contrast to NIMA and the closely related mammalian Nek2 kinase, which regulate centrosome function and separation, our data demonstrate an important function for Nek6 during mitosis and suggest that Nek6 kinase is required for metaphase-anaphase transition [3].
• Herein we show that Nek6 is increased in abundance and activity during mitosis; activation requires the phosphorylation of Ser206 on the Nek6 activation loop [2].
• Nek6 is phosphorylated and activated during M phase [3].

Biological context of NEK6

• Our analysis indicates that NEK6 has a strong preference for Leu 3 residues N-terminal to the site of phosphorylation [4].
• Recent work has implicated the NIMA (never in mitosis, gene A)-related kinase-6 (NEK6) as the enzyme that phosphorylates the hydrophobic motif of S6K1 in vivo [4].
• Employing the Jerini pepSTAR method in combination with kinetic analysis of phosphorylation of variant peptides, we establish the key substrate specificity determinants for NEK6 [4].
• Its open reading frame encodes a 302-amino acid protein and is 77% identical to human NEK6 protein [5].
• Assignment of NEK6, a NIMA-related gene, to human chromosome 9q33. 3-->q34.11 by radiation hybrid mapping [6].

Anatomical context of NEK6

• NEK7 expression was restricted to a subset of tissues containing lung, muscle, testis, brain, heart, liver, leukocyte, and spleen, but NEK6 transcripts were detected in all tissues studied [5].

Associations of NEK6 with chemical compounds

• The serine/threonine kinase Nek6 is required for cell cycle progression through mitosis [3].

Physical interactions of NEK6

• In this report, we found that Pin1 could interact with Nek6, one of the human NIMA-related kinases (Neks) [7].

Other interactions of NEK6

• We describe here the isolation of two novel murine protein kinase genes, designated nek6 and nek7, which are highly similar to each other (87% amino acid identity in the predicted kinase domain) [8].
• A newly identified S6 kinase kinase, NEK6, appears to provide the penultimate activation step [9].
• These findings support the conclusion that Nercc1/Nek9 and Nek6 represent a novel cascade of mitotic NIMA family protein kinases whose combined function is important for mitotic progression [2].

Analytical, diagnostic and therapeutic context of NEK6

• Tissue distributions of NEK7 and NEK6 were studied by RT-PCR [5].

References