The Mystery of Rap1 Suppression of Oncogenic Ras

Trends in Cancer - Tập 6 - Trang 369-379 - 2020
Ruth Nussinov1,2, Hyunbum Jang1, Mingzhen Zhang1, Chung-Jung Tsai1, Anna A. Sablina3
1Computational Structural Biology Section, Frederick National Laboratory for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702, USA
2Department of Human Molecular Genetics and Biochemistry, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel
3VIB Center for the Biology of Disease and KU Leuven Department of Oncology, Leuven Cancer Institute, Leuven, Belgium

Tài liệu tham khảo

Takahashi, 2017, Phosphorylation of Rap1 by cAMP-dependent protein kinase (PKA) creates a binding site for KSR to sustain ERK activation by cAMP, J. Biol. Chem., 292, 1449, 10.1074/jbc.M116.768986

Li, 2016, Protein kinase A-independent Ras protein activation cooperates with Rap1 protein to mediate activation of the extracellular signal-regulated kinases (ERK) by cAMP, J. Biol. Chem., 291, 21584, 10.1074/jbc.M116.730978

Xu, 2018, Small GTPase Rap1A/B is required for lymphatic development and adrenomedullin-induced stabilization of lymphatic endothelial junctions, Arterioscler. Thromb. Vasc. Biol., 38, 2410, 10.1161/ATVBAHA.118.311645

Raaijmakers, 2009, Specificity in Ras and Rap signaling, J. Biol. Chem., 284, 10995, 10.1074/jbc.R800061200

Itoh, 2007, Rap1 integrates tissue polarity, lumen formation, and tumorigenic potential in human breast epithelial cells, Cancer Res., 67, 4759, 10.1158/0008-5472.CAN-06-4246

Goto, 2010, Rap1 stabilizes β-catenin and enhances β-catenin-dependent transcription and invasion in squamous cell carcinoma of the head and neck, Clin. Cancer Res., 16, 65, 10.1158/1078-0432.CCR-09-1122

Okada, 1999, The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases, Mol. Cell. Biol., 19, 6057, 10.1128/MCB.19.9.6057

Stout, 2014, Analyzing Ras-associated cell proliferation signaling, Methods Mol. Biol., 1170, 393, 10.1007/978-1-4939-0888-2_21

Zhang, 2019, The mechanism of PI3Kα activation at the atomic level, Chem. Sci., 10, 3671, 10.1039/C8SC04498H

Xu, 2013, Dominant role of oncogene dosage and absence of tumor suppressor activity in Nras-driven hematopoietic transformation, Cancer Discov., 3, 993, 10.1158/2159-8290.CD-13-0096

Zhou, 2014, Signal integration by lipid-mediated spatial cross talk between Ras nanoclusters, Mol. Cell. Biol., 34, 862, 10.1128/MCB.01227-13

Fischer, 2007, B- and C-RAF display essential differences in their binding to Ras: the isotype-specific N terminus of B-RAF facilitates Ras binding, J. Biol. Chem., 282, 26503, 10.1074/jbc.M607458200

Williams, 2000, Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions, J. Biol. Chem., 275, 22172, 10.1074/jbc.M000397200

Lee, 2019, High-throughput single-particle tracking reveals nested membrane domains that dictate KRasG12D diffusion and trafficking, eLife, 8, 10.7554/eLife.46393

Wang, 2013, Mutant N-RAS protects colorectal cancer cells from stress-induced apoptosis and contributes to cancer development and progression, Cancer Discov., 3, 294, 10.1158/2159-8290.CD-12-0198

Cerami, 2012, The cBio Cancer Genomics Portal: an open platform for exploring multidimensional cancer genomics data, Cancer Discov., 2, 401, 10.1158/2159-8290.CD-12-0095