KLRG1 binds cadherins and preferentially associates with SHIP-1 (original) (raw)

Journal Article

Marlowe S. Tessmer ,

1Department of Molecular Microbiology and Immunology and Graduate Program in Pathobiology, Division of Biology and Medicine, Box G-B618, Brown University, Providence, RI 02912, USA

Search for other works by this author on:

Céline Fugere ,

1Department of Molecular Microbiology and Immunology and Graduate Program in Pathobiology, Division of Biology and Medicine, Box G-B618, Brown University, Providence, RI 02912, USA

Search for other works by this author on:

Frederik Stevenaert ,

2Department of Clinical Chemistry, Microbiology and Immunology, University of Ghent, Ghent, Belgium

Search for other works by this author on:

Olga V. Naidenko ,

3Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, USA

Search for other works by this author on:

H. Jonathan Chong ,

1Department of Molecular Microbiology and Immunology and Graduate Program in Pathobiology, Division of Biology and Medicine, Box G-B618, Brown University, Providence, RI 02912, USA

Search for other works by this author on:

Georges Leclercq ,

2Department of Clinical Chemistry, Microbiology and Immunology, University of Ghent, Ghent, Belgium

Search for other works by this author on:

Laurent Brossay

1Department of Molecular Microbiology and Immunology and Graduate Program in Pathobiology, Division of Biology and Medicine, Box G-B618, Brown University, Providence, RI 02912, USA

Search for other works by this author on:

Received:

11 December 2006

Accepted:

15 January 2007

Published:

16 February 2007

• • Article contents
  • Figures & tables
  • Video
  • Audio
  • Supplementary Data
• Cite

Cite

Marlowe S. Tessmer, Céline Fugere, Frederik Stevenaert, Olga V. Naidenko, H. Jonathan Chong, Georges Leclercq, Laurent Brossay, KLRG1 binds cadherins and preferentially associates with SHIP-1, International Immunology, Volume 19, Issue 4, April 2007, Pages 391–400, https://doi.org/10.1093/intimm/dxm004
Close

Navbar Search Filter Mobile Enter search term Search

Abstract

The killer cell lectin-like receptor G1 (KLRG1) is a unique inhibitory receptor expressed on a phenotypically mature subset of resting NK cells as well as subsets of T cells in naive mice. In vivo, pathogenic immune system activation induces dramatic changes in the expression patterns of KLRG1 among the different cell subsets. In order to enhance our understanding of KLRG1 signaling properties and to clarify the functions of KLRG1 on these cells, we identified the broadly expressed N-cadherin molecule as a ligand for KLRG1. We further demonstrate that a second member of this superfamily of adhesion molecules, E-cadherin, binds to KLRG1. Additionally, we show that upon phosphorylation of the immunoreceptor tyrosine-based inhibitory motif (ITIM) tyrosine, KLRG1 recruits both SHIP-1 and SHP-2 but not SHP-1. We also delineate the key KLRG1 ITIM amino acid residues required for optimal association with these phosphatases. Finally, we demonstrate that KLRG1 engagement can inhibit sub-optimal TCR signaling. Taken together, our results indicate that KLRG1 may differentially regulate NK cell and T cell functions through the association with different ligands as well as the recruitment of distinct phosphatases.

© The Japanese Society for Immunology. 2007. All rights reserved. For permissions, please e-mail: [email protected]

Topic:

• signal transduction
• amino acids
• cadherins
• natural killer cells
• ligands
• phosphoric monoester hydrolases
• phosphorylation
• ships
• t-lymphocytes
• mice
• tyrosine
• e-cadherin
• hematopoietic cell phosphatase
• n-cadherins
• binding (molecular function)
• molecule

You do not currently have access to this article.

Personal account

• Sign in with email/username & password
• Get email alerts
• Save searches
• Purchase content
• Activate your purchase/trial code
• Add your ORCID iD

Get help with access

Institutional access

Access to content on Oxford Academic is often provided through institutional subscriptions and purchases. If you are a member of an institution with an active account, you may be able to access content in one of the following ways:

IP based access

Typically, access is provided across an institutional network to a range of IP addresses. This authentication occurs automatically, and it is not possible to sign out of an IP authenticated account.

Sign in through your institution

Choose this option to get remote access when outside your institution. Shibboleth/Open Athens technology is used to provide single sign-on between your institution's website and Oxford Academic.

1. Click Sign in through your institution.
2. Select your institution from the list provided, which will take you to your institution's website to sign in.
3. When on the institution site, please use the credentials provided by your institution. Do not use an Oxford Academic personal account.
4. Following successful sign in, you will be returned to Oxford Academic.

If your institution is not listed or you cannot sign in to your institution's website, please contact your librarian or administrator.

Sign in with a library card

Enter your library card number to sign in. If you cannot sign in, please contact your librarian.

Society Members

Society member access to a journal is achieved in one of the following ways:

Sign in through society site

Many societies offer single sign-on between the society website and Oxford Academic. If you see "Sign in through society site" in the sign in pane within a journal:

1. Click Sign in through society site.
2. When on the society site, please use the credentials provided by that society. Do not use an Oxford Academic personal account.
3. Following successful sign in, you will be returned to Oxford Academic.

If you do not have a society account or have forgotten your username or password, please contact your society.

Sign in using a personal account

Some societies use Oxford Academic personal accounts to provide access to their members. See below.

Personal account

A personal account can be used to get email alerts, save searches, purchase content, and activate subscriptions.

Some societies use Oxford Academic personal accounts to provide access to their members.

Viewing your signed in accounts

Click the account icon in the top right to:

• View your signed in personal account and access account management features.
• View the institutional accounts that are providing access.

Signed in but can't access content

Oxford Academic is home to a wide variety of products. The institutional subscription may not cover the content that you are trying to access. If you believe you should have access to that content, please contact your librarian.

Institutional account management

For librarians and administrators, your personal account also provides access to institutional account management. Here you will find options to view and activate subscriptions, manage institutional settings and access options, access usage statistics, and more.

Purchase

Short-term Access

To purchase short-term access, please sign in to your personal account above.

Don't already have a personal account? Register

KLRG1 binds cadherins and preferentially associates with SHIP-1 - 24 Hours access

EUR €53.00

GBP £44.00

USD $58.00

Rental

This article is also available for rental through DeepDyve.

Advertisement intended for healthcare professionals

Advertisement intended for healthcare professionals