On the relationship status for Arf and NPM1 – it's complicated

On the relationship status for Arf and NPM1 – it's complicated AbbreviationsNPM1NucleophosminR‐motifarginine‐rich short linear motifThe nucleolar protein nucleophosmin (NPM1) and tumor suppressor protein p14Arf interact and function together in tumor suppression and cellular stress sensing pathways. Although known for more than a decade, characterization of the structural mechanism of this interaction has been challenging. In this issue of The FEBS Journal, Luchinat, et al. , provide new insights into this elusive interaction.Human p14Arf protein (p19Arf in mice) is intrinsically disordered , the translational product of an alternative reading frame within the Ink4a locus on chromosome 9p21, which also encodes the cyclin‐dependent kinase inhibitor, p16Ink4A . These two structurally and functionally unrelated proteins are the product of alternative first exons and share second and third exons (Fig. A), and they mediate tumor suppression through independent mechanisms .An alternative reading frame within the Ink4a locus encodes a disordered, polycationic protein. (A) Ink4a locus encodes for two unrelated tumor suppressor proteins, p14Arf and p16Ink4A; exons encoding for Arf and p16Ink4A are color‐coded blue and purple, respectively. Dual colored exons represent overlap coding regions. (B) Net charge per residue analysis (prepared using CIDER, http://pappulab.wustl.edu/CIDER/) of the human (p14Arf) and mouse (p19Arf) protein sequences. Charge distribution in the C‐terminal region of p19Arf is more uniform compared to http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Febs Journal Wiley

On the relationship status for Arf and NPM1 – it's complicated

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
Copyright © 2018 Federation of European Biochemical Societies
ISSN
1742-464X
eISSN
1742-4658
D.O.I.
10.1111/febs.14407
Publisher site
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Abstract

AbbreviationsNPM1NucleophosminR‐motifarginine‐rich short linear motifThe nucleolar protein nucleophosmin (NPM1) and tumor suppressor protein p14Arf interact and function together in tumor suppression and cellular stress sensing pathways. Although known for more than a decade, characterization of the structural mechanism of this interaction has been challenging. In this issue of The FEBS Journal, Luchinat, et al. , provide new insights into this elusive interaction.Human p14Arf protein (p19Arf in mice) is intrinsically disordered , the translational product of an alternative reading frame within the Ink4a locus on chromosome 9p21, which also encodes the cyclin‐dependent kinase inhibitor, p16Ink4A . These two structurally and functionally unrelated proteins are the product of alternative first exons and share second and third exons (Fig. A), and they mediate tumor suppression through independent mechanisms .An alternative reading frame within the Ink4a locus encodes a disordered, polycationic protein. (A) Ink4a locus encodes for two unrelated tumor suppressor proteins, p14Arf and p16Ink4A; exons encoding for Arf and p16Ink4A are color‐coded blue and purple, respectively. Dual colored exons represent overlap coding regions. (B) Net charge per residue analysis (prepared using CIDER, http://pappulab.wustl.edu/CIDER/) of the human (p14Arf) and mouse (p19Arf) protein sequences. Charge distribution in the C‐terminal region of p19Arf is more uniform compared to

Journal

Febs JournalWiley

Published: Jan 1, 2018

References

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