The Ability of Sos1 to Oligomerize the Adaptor Protein LAT Is Separable from Its Guanine Nucleotide Exchange Activity in Vivo-Reference-Cited by-同舟云学术

The Ability of Sos1 to Oligomerize the Adaptor Protein LAT Is Separable from Its Guanine Nucleotide Exchange Activity in Vivo

Published:2013-11-12 Issue:301 Volume:6 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Kortum Robert L.¹,Balagopalan Lakshmi¹,Alexander Clayton P.¹,Garcia Julie¹,Pinski John M.¹,Merrill Robert K.¹,Nguyen Phan H.¹,Li Wenmei¹,Agarwal Isha¹,Akpan Itoro O.¹,Sommers Connie L.¹,Samelson Lawrence E.¹

Affiliation:

1. Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.

Abstract

Thymocyte development requires that Sos1 acts both as a guanine nucleotide exchange factor and as a scaffold to cluster adaptor proteins.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference46 articles.

1. Ras and extracellular signal-regulated kinase signaling in thymocytes and T cells

2. Structural Evidence for Feedback Activation by Ras·GTP of the Ras-Specific Nucleotide Exchange Factor SOS

3. Digital Signaling and Hysteresis Characterize Ras Activation in Lymphoid Cells

4. Unusual Interplay of Two Types of Ras Activators, RasGRP and SOS, Establishes Sensitive and Robust Ras Activation in Lymphocytes

5. Decision checkpoints in the thymus

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