Next Article in Journal
Glucagon-Induced Acetylation of Energy-Sensing Factors in Control of Hepatic Metabolism
Previous Article in Journal
Considerations for the Use of Polyphenols as Therapies in Neurodegenerative Diseases
Previous Article in Special Issue
A Molecular Dynamics Approach to Explore the Intramolecular Signal Transduction of PPAR-α
Article Menu
Issue 8 (April-2) cover image

Export Article

Open AccessArticle

Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells

Laboratory of Structural Biology and Cell Signaling, Institute of Microbiology, The Czech Academy of Sciences, Vídeňská 1083, 14220 Prague 4, Czech Republic
Department of Biophysical Chemistry, J. Heyrovsky Institute of Physical Chemistry, The Czech Academy of Sciences, Dolejškova 2155/3, 18223 Prague 8, Czech Republic
Department of Biochemistry, Charles University, Hlavova 8, 12843 Prague 2, Czech Republic
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(8), 1884;
Received: 12 March 2019 / Revised: 4 April 2019 / Accepted: 10 April 2019 / Published: 16 April 2019
(This article belongs to the Special Issue Protein Structural Dynamics 2019)
PDF [4836 KB, uploaded 16 April 2019]
  |     |  


Mouse activating Nkrp1 proteins are commonly described as type II transmembrane receptors with disulfide-linked homodimeric structure. Their function and the manner in which Nkrp1 proteins of mouse strain (C57BL/6) oligomerize are still poorly understood. To assess the oligomerization state of Nkrp1 proteins, mouse activating EGFP-Nkrp1s were expressed in mammalian lymphoid cells and their oligomerization evaluated by Förster resonance energy transfer (FRET). Alternatively, Nkrp1s oligomers were detected by Western blotting to specify the ratio between monomeric and dimeric forms. We also performed structural characterization of recombinant ectodomains of activating Nkrp1 receptors. Nkrp1 isoforms c1, c2 and f were expressed prevalently as homodimers, whereas the Nkrp1a displays larger proportion of monomers on the cell surface. Cysteine-to-serine mutants revealed the importance of all stalk cysteines for protein dimerization in living cells with a major influence of cysteine at position 74 in two Nkrp1 protein isoforms. Our results represent a new insight into the oligomerization of Nkrp1 receptors on lymphoid cells, which will help to determine their function. View Full-Text
Keywords: Nkrp1; dimerization; Förster resonance energy transfer; disulfide bond arrangement; cysteine Nkrp1; dimerization; Förster resonance energy transfer; disulfide bond arrangement; cysteine

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Adámková, L.; Kvíčalová, Z.; Rozbeský, D.; Kukačka, Z.; Adámek, D.; Cebecauer, M.; Novák, P. Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells. Int. J. Mol. Sci. 2019, 20, 1884.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top