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RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi

  1. Author:
    Lee, D.
    Walsh, J. D.
    Mikhailenko, I.
    Yu, P.
    Migliorini, M.
    Wu, Y. B.
    Krueger, S.
    Curtis, J. E.
    Harris, B.
    Lockett, S.
    Blacklow, S. C.
    Strickl, D. K.
    Wang, Y. X.

  2. Author Address

    Univ Maryland, Sch Med, Ctr Vasc & Inflammatory Dis, Dept Surg, Baltimore, MD 21201 USA. Univ Maryland, Sch Med, Ctr Vasc & Inflammatory Dis, Dept Physiol, Baltimore, MD 21201 USA. Natl Inst Stand & Technol, Ctr Neutron Res, Gaithersburg, MD 20899 USA. Brigham & Womens Hosp, Dept Pathol, Boston, MA 02115 USA. NCI, Struct Res Program, Prot Nucle Acid Interact Sect, NIH, Frederick, MD 21702 USA. NCI, Basic Res Program, NIH, Frederick, MD 21702 USA. NCI, SAIC Frederick Inc, Res Technol Program, NIH, Frederick, MD 21702 USA Strickland, DK, Univ Maryland, Sch Med, Ctr Vasc & Inflammatory Dis, Dept Surg, Baltimore, MD 21201 USA
    1. Year: 2006
    2. Date: MAY 5
  2. Journal: Molecular Cell
    1. 22
    2. 3
    3. Pages: 423-430
  4. Type of Article: Article
  1. Abstract:

    The receptor associated protein (RAP) is an antagonist and molecular chaperone that binds tightly to low-density lipoprotein receptor family members in the endoplasmic reticulum (ER). After escorting these receptors to the Golgi, RAP dissociates from the receptors. The molecular mechanism of the dissociation has been unknown until now. The solution structure of RAP-D3 domain presented here reveals a striking increase in positively charged residues on the surface of this RAP domain due to protonation of solvent-xposed histidine sidechains as the pH is reduced from a near neutral pH of the ER to the acidic pH of the Golgi. Structure-based mutagenesis studies in vitro and in cells confirm that the protonation of histidine residues as a consequence of the pH changes modulate the binding/release of RAP from LRP. This histidine switch may serve as a general mechanism for regulating cell trafficking events

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  2. DOI: 10.1016/j.molcel.2006.04.011
  3. View record in Web of Science®
  4. WOS: 000237618200013

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