» Articles » PMID: 21863376

Cis-trans Interactions of Cell Surface Receptors: Biological Roles and Structural Basis

Overview
Publisher Springer
Specialty Biology
Date 2011 Aug 25
PMID 21863376
Citations 25
Authors
Affiliations
Soon will be listed here.
Abstract

Cell surface receptors bind ligands expressed on other cells (in trans) in order to communicate with neighboring cells. However, an increasing number of cell surface receptors are found to also interact with ligands expressed on the same cell (in cis). These observations raise questions regarding the biological role of such cis interactions. Specifically, it is important to know whether cis and trans binding have distinct functional effects and, if so, how a single cell discriminates between interactions in cis versus trans. Further, what are the structural features that allow certain cell surface receptors to engage ligand both on the same as well as on an apposed cell membrane? Here, we summarize known examples of receptors that display cis-trans binding and discuss the emerging diversity of biological roles played by these unconventional two-way interactions, along with their structural basis.

Citing Articles

Recognition of Self and Viral Ligands by NK Cell Receptors.

Mariuzza R, Singh P, Karade S, Shahid S, Sharma V Immunol Rev. 2025; 329(1):e13435.

PMID: 39748148 PMC: 11695704. DOI: 10.1111/imr.13435.


Genetic and functional diversity of allorecognition receptors in the urochordate, .

Rodriguez-Valbuena H, Salcedo J, De Their O, Flot J, Tiozzo S, De Tomaso A bioRxiv. 2024; .

PMID: 39463968 PMC: 11507803. DOI: 10.1101/2024.10.16.618699.


Ephs in cancer progression: complexity and context-dependent nature in signaling, angiogenesis and immunity.

Guo X, Yang Y, Tang J, Xiang J Cell Commun Signal. 2024; 22(1):299.

PMID: 38811954 PMC: 11137953. DOI: 10.1186/s12964-024-01580-3.


Notch ligands are biomarkers of anti-TNF response in RA patients.

Zack S, Meyer A, Zanotti B, Volin M, Deen S, Satoeya N Angiogenesis. 2023; 27(2):273-283.

PMID: 37796367 PMC: 10995106. DOI: 10.1007/s10456-023-09897-2.


Recent developments in the cleavage, functionalization, and conjugation of proteins and peptides at tyrosine residues.

Zhang S, De Leon Rodriguez L, Li F, Brimble M Chem Sci. 2023; 14(29):7782-7817.

PMID: 37502317 PMC: 10370606. DOI: 10.1039/d3sc02543h.


References
1.
Fourmentraux-Neves E, Jalil A, Da Rocha S, Pichon C, Chouaib S, Bismuth G . Two opposite signaling outputs are driven by the KIR2DL1 receptor in human CD4+ T cells. Blood. 2008; 112(6):2381-9. DOI: 10.1182/blood-2007-12-127779. View

2.
Mori Y, Tsuji S, Inui M, Sakamoto Y, Endo S, Ito Y . Inhibitory immunoglobulin-like receptors LILRB and PIR-B negatively regulate osteoclast development. J Immunol. 2008; 181(7):4742-51. DOI: 10.4049/jimmunol.181.7.4742. View

3.
Matsumoto N, Mitsuki M, Tajima K, Yokoyama W, Yamamoto K . The functional binding site for the C-type lectin-like natural killer cell receptor Ly49A spans three domains of its major histocompatibility complex class I ligand. J Exp Med. 2001; 193(2):147-58. PMC: 2193338. DOI: 10.1084/jem.193.2.147. View

4.
Colonna M, Navarro F, Bellon T, Llano M, Garcia P, Samaridis J . A common inhibitory receptor for major histocompatibility complex class I molecules on human lymphoid and myelomonocytic cells. J Exp Med. 1998; 186(11):1809-18. PMC: 2199153. DOI: 10.1084/jem.186.11.1809. View

5.
Haklai-Topper L, Mlechkovich G, Savariego D, Gokhman I, Yaron A . Cis interaction between Semaphorin6A and Plexin-A4 modulates the repulsive response to Sema6A. EMBO J. 2010; 29(15):2635-45. PMC: 2928682. DOI: 10.1038/emboj.2010.147. View