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Organization of Farnesylated, Carboxymethylated KRAS4B on Membranes

  1. Author:
    Barklis, Eric
    Stephen,Andy
    Staubus, August O
    Barklis, Robin Lid
    Alfadhli, Ayna

  2. Author Address

    Department of Molecular Microbiology and Immunology, Oregon Health & Sciences University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239. Electronic address: barklis@ohsu.edu., NCI RAS Initiative, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD 21072, United States of America.,
    1. Year: 2019
    2. Date: SEP 6
    3. Epub Date: 2019 07 19
  2. Journal: Journal of molecular biology
    1. 431
    2. 19
    3. Pages: 3706-3717
  4. Type of Article: Article
  5. ISSN: 0022-2836
  1. Abstract:

    Mutations of the Ras proteins HRAS, KRAS4A, KRAS4B, and NRAS are associated with a high percentage of all human cancers. The proteins are composed of highly homologous N-terminal catalytic or globular domains, plus C-terminal hypervariable regions (HVRs). Post-translational modifications of all RAS HVRs helps target RAS proteins to cellular membrane locations where they perform their signaling functions. For the predominant KRAS4 isoform, KRAS4B, post-translational farnesylation and carboxymethylation, along with a patch of HVR basic residues help foster membrane binding. Recent investigations implicate membrane-bound RAS dimers, oligomers and nanoclusters as landing pads for effector proteins that relay RAS signals. The details of these RAS signaling platforms have not been elucidated completely, in part due to the difficulties in preparing modified proteins. We have employed properly farnesylated and carboxymethylated KRAS4B in lipid monolayer incubations to examine how the proteins assemble on membranes. Our results reveal novel insights as to how KRAS4B may organize on membranes. Copyright © 2019. Published by Elsevier Ltd.

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External Sources

  1. View Full Text
  2. DOI: 10.1016/j.jmb.2019.07.025
  3. PMID: 31330153
  4. View record in Web of Science®
  5. WOS: 000487168300008
  6. PII : S0022-2836(19)30456-5

Library Notes

  1. Fiscal Year: FY2018-2019
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