High impact information on MTR10

• This import defect can be reversed by increasing the intracellular concentration of Mtr10p, the nuclear import receptor for Npl3p [1].
• MTR10, previously shown to be involved in mRNA export, was found in a synthetic lethal relationship with nucleoporin NUP85 [2].
• Mtr10p interacts in vitro with Gsp1p-GTP, but with low affinity [2].
• Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p [2].
• Green fluorescent protein (GFP)-tagged Mtr10p localizes preferentially inside the nucleus, but a nuclear pore and cytoplasmic distribution is also evident [2].

Biological context of MTR10

• Finally, TAB1 was shown to be MTR10, a gene encoding nuclear transport receptor/adaptor [3].
• The RGG motif is also methylated on arginine residues, but methylation does not affect the Npl3p-Mtr10p interaction in vitro [4].
• We found that the latter is the site for phosphorylation by Sky1p and that this phosphorylation regulates nuclear import of Npl3p by modulating the interaction of the RGG motif with its nuclear import receptor Mtr10p [4].
• Biogenesis of yeast telomerase depends on the importin mtr10 [5].

Associations of MTR10 with chemical compounds

• Moreover, using sucrose density gradient analysis, we provide evidence that the import receptor Mtr10p, but not the SR protein kinase Sky1p, is involved in the timely regulated release of Npl3p from polysome-associated mRNAs [6].

Physical interactions of MTR10

• Purified Mtr10p forms a complex with Npl3p, an RNA-binding protein that shuttles in and out of the nucleus [2].

Other interactions of MTR10

• Hrb1 is nuclear at steady state and its import is mediated by the karyopherin Mtr10 [7].
• The redistribution of Npl3p is accompanied by its increased association with poly(A)+ RNA and decreased association with its import receptor, Mtr10p, in vivo [8].
• MA utilizes Kap120p and Mtr10p import receptors while nuclear entry of NC involves the classical importin-alpha/beta (Kap60p/95p) pathway [9].

References