The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Intracellular signalling controlling integrin activation in lymphocytes
Abstract
Since the discovery that integrins at the surface of lymphocytes undergo dynamic changes in their adhesive activity after stimulation through the T-cell receptor or stimulation with chemokines, intensive research has been carried out in an attempt to clarify the signalling events that lead to the activation of integrins. Whereas structural studies have provided us with a vivid picture of the conformational flexibility of integrins, the signalling pathways that regulate these conformational changes (known as inside-out signalling) have been elusive. However, as I discuss here, recent studies have provided new insight into the pathways that control the regulation of integrin activity and the coordination of complex cellular functions, such as the homing of lymphocytes and the formation of an immunological synapse.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Atypical Rho GTPases, including RHOH, lack GTPase activity and therefore remain in the active, GTP-bound conformation (20,21).”
From Human RHOH deficiency causes T cell defects and susceptibility to EV-HPV infections (2012) · cites this paper as [21]
Citations
Cites
Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration
Fukui, Y., Hashimoto, O., Sanui, T., Oono, T., Koga, H., Abe, M., Inayoshi, A., Noda, M., Oike, M., Shirai, T., et al. (2001) · Nature · doi:10.1038/35090591 · Cited by 449
Li, X., Bu, X., Lu, B., Avraham, H., Flavell, R. A., & Lim, B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1158-1171.2002 · Cited by 153
Research works printed but not linked: 127
- Hemler, M. E. VLA proteins in the integrin family: structures, functions, and their role on leukocytes. Annu. Rev. Immunol. 8, 365–400 (1990). · DOI
- Hynes, R. O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11–25 (1992). · DOI
- Springer, T. A. Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration. Annu. Rev. Physiol. 57, 827–872 (1995). · DOI
- Butcher, E. C., Williams, M., Youngman, K., Rott, L. & Briskin, M. Lymphocyte trafficking and regional immunity. Adv. Immunol. 72, 209–253 (1999). · DOI
- Dustin, M. L. & Springer, T. A. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature 341, 619–624 (1989). · DOI
- Carman, C. V. & Springer, T. A. Integrin avidity regulation: are changes in affinity and conformation underemphasized? Curr. Opin. Cell Biol. 15, 547–556 (2003). · DOI
- Bazzoni, G. & Hemler, M. E. Are changes in integrin affinity and conformation overemphasized? Trends Biochem. Sci. 23, 30–34 (1998). · DOI
- Grakoui, A. et al. The immunological synapse: a molecular machine controlling T cell activation. Science 285, 221–226 (1999). · DOI
- Monks, C. R., Freiberg, B. A., Kupfer, H., Sciaky, N. & Kufper, A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 395, 82–86 (1998). · DOI · Paper page
- Bachmann, M. F. et al. Distinct roles for LFA-1 and CD28 during activation of naive T cells: adhesion versus costimulation. Immunity 7, 549–557 (1997). · DOI
- Kucik, D. F., Dustin, M. L., Miller, J. M. & Brown, E. J. Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. J. Clin. Invest. 97, 2139–2144 (1996). · DOI
- Yauch, R. L. et al. Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independence of ligand binding. J. Exp. Med. 186, 1347–1355 (1997). · DOI
- Chan, J. R., Hyduk, S. J. & Cybulsky, M. I. Chemoattractants induce a rapid and transient upregulation of monocyte α4 integrin affinity for vascular cell adhesion molecule 1 which mediates arrest: an early step in the process of emigration. J. Exp. Med. 193, 1149–1158 (2001). · DOI
- Lollo, B. A., Chan, K. W., Hanson, E. M., Moy, V. T. & Brian, A. A. Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated T cells. J. Biol. Chem. 268, 21693–21700 (1993). · DOI
- Constantin, G. et al. Chemokines trigger immediate β2 integrin affinity and mobility changes: differential regulation and roles in lymphocyte arrest under flow. Immunity 13, 759–769 (2000). · DOI
- Takagi, J. & Springer, T. A. Integrin activation and structural rearrangement. Immunol. Rev. 186, 141–163 (2002). · DOI
- Lee, J. O., Bankston, L. A., Arnaout, M. A. & Liddington, R. C. Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure 3, 1333–1340 (1995). · DOI
- Shimaoka, M. et al. Structures of the αL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Cell 112, 99–111 (2003). · DOI
- Emsley, J., Knight, C. G., Farndale, R. W., Barnes, M. J. & Liddington, R. C. Structural basis of collagen recognition by integrin α2β1 . Cell 101, 47–56 (2000). · DOI
- Xiong, J. P. et al. Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science 296, 151–155 (2002). · DOI
- Takagi, J., Petre, B. M., Walz, T. & Springer, T. A. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 110, 599–611 (2002). This is the landmark study of the global structural changes in integrins that are associated with ligand binding and occur after cellular activation. · DOI
- Adair, B. D. et al. Three-dimensional EM structure of the ectodomain of integrin αVβ3 in a complex with fibronectin. J. Cell Biol. 168, 1109–1118 (2005). · DOI
- Dustin, M. L., Bivona, T. G. & Philips, M. R. Membranes as messengers in T cell adhesion signaling. Nature Immunol. 5, 363–372 (2004). · DOI
- Lu, C., Ferzly, M., Takagi, J. & Springer, T. A. Epitope mapping of antibodies to the C-terminal region of the integrin β2 subunit reveals regions that become exposed upon receptor activation. J. Immunol. 166, 5629–5637 (2001). · DOI
- Vinogradova, O. et al. A structural mechanism of integrin αIIbβ3 'inside-out' activation as regulated by its cytoplasmic face. Cell 110, 587–597 (2002). · DOI
- Hughes, P. E. et al. Breaking the integrin hinge. J. Biol. Chem. 271, 6571–6574 (1996). · DOI
- Kim, M., Carman, C. V. & Springer, T. A. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301, 1720–1725 (2003). Using FRET technology, this study showed that the cytoplasmic regions of LFA1 separate after ligand binding and cellular activation. · DOI · Paper page
- Horwitz, A., Duggan, K., Buck, C., Beckerle, M. C. & Burridge, K. Interaction of plasma membrane fibronectin receptor with talin — a transmembrane linkage. Nature 320, 531–533 (1986). · DOI
- Burridge, K. & Connell, L. Talin: a cytoskeletal component concentrated in adhesion plaques and other sites of actin–membrane interaction. Cell Motil. 3, 405–417 (1983). · DOI
- Gomez-Mouton, C. et al. Segregation of leading-edge and uropod components into specific lipid rafts during T cell polarization. Proc. Natl Acad. Sci. USA 98, 9642–9647 (2001). · DOI
- Rees, D. J., Ades, S. E., Singer, S. J. & Hynes, R. O. Sequence and domain structure of talin. Nature 347, 685–689 (1990). · DOI
- Garcia-Alvarez, B. et al. Structural determinants of integrin recognition by talin. Mol. Cell 11, 49–58 (2003). · DOI
- Tadokoro, S. et al. Talin binding to integrin β tails: a final common step in integrin activation. Science 302, 103–106 (2003). · DOI
- Pearson, M. A., Reczek, D., Bretscher, A. & Karplus, P. A. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 101, 259–270 (2000). · DOI
- Calderwood, D. A. et al. The talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation. J. Biol. Chem. 274, 28071–28074 (1999). · DOI · Paper page
- Yan, B., Calderwood, D. A., Yaspan, B. & Ginsberg, M. H. Calpain cleavage promotes talin binding to the β3 integrin cytoplasmic domain. J. Biol. Chem. 276, 28164–28170 (2001). · DOI
- Stewart, M. P., McDowall, A. & Hogg, N. LFA-1-mediated adhesion is regulated by cytoskeletal restraint and by a Ca2+-dependent protease, calpain. J. Cell Biol. 140, 699–707 (1998). · DOI
- Sampath, R., Gallagher, P. J. & Pavalko, F. M. Cytoskeletal interactions with the leukocyte integrin β2 cytoplasmic tail. Activation-dependent regulation of associations with talin and α-actinin. J. Biol. Chem. 273, 33588–33594 (1998). · DOI
- Stein, J. V. et al. The CC chemokine thymus-derived chemotactic agent 4 (TCA-4, secondary lymphoid tissue chemokine, 6Ckine, exodus-2) triggers lymphocyte function-associated antigen 1-mediated arrest of rolling T lymphocytes in peripheral lymph node high endothelial venules. J. Exp. Med. 191, 61–76 (2000). · DOI
- Warnock, R. A. et al. The role of chemokines in the microenvironmental control of T versus B cell arrest in Peyer's patch high endothelial venules. J. Exp. Med. 191, 77–88 (2000). · DOI
- Okada, T. et al. Chemokine requirements for B cell entry to lymph nodes and Peyer's patches. J. Exp. Med. 196, 65–75 (2002). · DOI
- Ebisuno, Y. et al. The B cell chemokine CXC chemokine ligand 13/B lymphocyte chemoattractant is expressed in the high endothelial venules of lymph nodes and Peyer's patches and affects B cell trafficking across high endothelial venules. J. Immunol. 171, 1642–1646 (2003). · DOI
- Grabovsky, V. et al. Subsecond induction of α4 integrin clustering by immobilized chemokines stimulates leukocyte tethering and rolling on endothelial vascular cell adhesion molecule 1 under flow conditions. J. Exp. Med. 192, 495–506 (2000). · DOI
- Chan, J. R., Hyduk, S. J. & Cybulsky, M. I. Detecting rapid and transient upregulation of leukocyte integrin affinity induced by chemokines and chemoattractants. J. Immunol. Methods 273, 43–52 (2003). · DOI
- Salas, A., Shimaoka, M., Chen, S., Carman, C. V. & Springer, T. Transition from rolling to firm adhesion is regulated by the conformation of the I domain of the integrin lymphocyte function-associated antigen-1. J. Biol. Chem. 277, 50255–50262 (2002). · DOI
- Atarashi, K., Hirata, T., Matsumoto, M., Kanemitsu, N. & Miyasaka, M. Rolling of TH1 cells via P-selectin glycoprotein ligand-1 stimulates LFA-1-mediated cell binding to ICAM-1. J. Immunol. 174, 1424–1432 (2005). · DOI
- Shamri, R. et al. Lymphocyte arrest requires instantaneous induction of an extended LFA-1 conformation mediated by endothelium-bound chemokines. Nature Immunol. 6, 497–506 (2005). This paper was the first to show that extension of LFA1 triggered by immobilized chemokines is the crucial step in mediating lymphocyte arrest under shear-flow conditions. · DOI
- Miller, M. J., Wei, S. H., Parker, I. & Cahalan, M. D. Two-photon imaging of lymphocyte motility and antigen response in intact lymph node. Science 296, 1869–1873 (2002). · DOI
- Moser, B., Wolf, M., Walz, A. & Loetscher, P. Chemokines: multiple levels of leukocyte migration control. Trends Immunol. 25, 75–84 (2004). · DOI
- Lo, C. G., Lu, T. T. & Cyster, J. G. Integrin-dependence of lymphocyte entry into the splenic white pulp. J. Exp. Med. 197, 353–361 (2003). · DOI
- Bousso, P. & Robey, E. Dynamics of CD8+ T cell priming by dendritic cells in intact lymph nodes. Nature Immunol. 4, 579–585 (2003). · DOI
- Mempel, T. R., Henrickson, S. E. & Von Andrian, U. H. T-cell priming by dendritic cells in lymph nodes occurs in three distinct phases. Nature 427, 154–159 (2004). · DOI
- Miller, M. J., Safrina, O., Parker, I. & Cahalan, M. D. Imaging the single cell dynamics of CD4+ T cell activation by dendritic cells in lymph nodes. J. Exp. Med. 200, 847–856 (2004). · DOI
- Sanchez-Madrid, F. & del Pozo, M. A. Leukocyte polarization in cell migration and immune interactions. EMBO J. 18, 501–511 (1999). · DOI
- Ward, S. G. Do phosphoinositide 3-kinases direct lymphocyte navigation? Trends Immunol. 25, 67–74 (2004). · DOI
- Shimizu, Y., Mobley, J. L., Finkelstein, L. D. & Chan, A. S. A role for phosphatidylinositol 3-kinase in the regulation of β1 integrin activity by the CD2 antigen. J. Cell Biol. 131, 1867–1880 (1995). · DOI
- Zell, T., Hunt, S. W., Mobley, J. L., Finkelstein, L. D. & Shimizu, Y. CD28-mediated up-regulation of β1-integrin adhesion involves phosphatidylinositol 3-kinase. J. Immunol. 156, 883–886 (1996). · DOI
- Kinashi, T., Escobedo, J. A., Williams, L. T., Takatsu, K. & Springer, T. A. Receptor tyrosine kinase stimulates cell-matrix adhesion by phosphatidylinositol 3 kinase and phospholipase C-γ1 pathways. Blood 86, 2086–2090 (1995). · DOI
- Kinashi, T., Asaoka, T., Setoguchi, R. & Takatsu, K. Affinity modulation of very late antigen-5 through phosphatidylinositol 3-kinase in mast cells. J. Immunol. 162, 2850–2857 (1999). · DOI
- Katagiri, K. et al. Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-kinase. Mol. Cell. Biol. 20, 1956–1969 (2000). · DOI
- Li, Z. et al. Roles of PLC-β2 and -β3 and PI3Kγ in chemoattractant-mediated signal transduction. Science 287, 1046–1049 (2000). · DOI
- Hirsch, E. et al. Central role for G protein-coupled phosphoinositide 3-kinase γ in inflammation. Science 287, 1049–1053 (2000). · DOI
- Reif, K. et al. Differential roles for phosphoinositide 3-kinases, p110γ and p110δ, in lymphocyte chemotaxis and homing. J. Immunol. 173, 2236–2240 (2004). · DOI
- Okkenhaug, K. & Vanhaesebroeck, B. PI3K in lymphocyte development, differentiation and activation. Nature Rev. Immunol. 3, 317–330 (2003). · DOI
- Nombela-Arrieta, C. et al. Differential requirements for DOCK2 and phosphoinositide-3-kinase γ during T and B lymphocyte homing. Immunity 21, 429–441 (2004). This study showed that a deficiency in DOCK2 impairs the LFA1-dependent tethering and firm adhesion to endothelial venules of B cells but not T cells. · DOI
- Kolanus, W. et al. αLβ2 Integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell 86, 233–242 (1996). · DOI
- Meacci, E., Tsai, S. C., Adamik, R., Moss, J. & Vaughan, M. Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc. Natl Acad. Sci. USA 94, 1745–1748 (1997). · DOI
- Weber, K. S. et al. Cytohesin-1 is a dynamic regulator of distinct LFA-1 functions in leukocyte arrest and transmigration triggered by chemokines. Curr. Biol. 11, 1969–1974 (2001). · DOI
- Perez, O. D. et al. Leukocyte functional antigen 1 lowers T cell activation thresholds and signaling through cytohesin-1 and Jun-activating binding protein 1. Nature Immunol. 4, 1083–1092 (2003). · DOI
- Laudanna, C., Campbell, J. J. & Butcher, E. C. Role of Rho in chemoattractant-activated leukocyte adhesion through integrins. Science 271, 981–983 (1996). · DOI
- Giagulli, C. et al. RhoA and ζ PKC control distinct modalities of LFA-1 activation by chemokines: critical role of LFA-1 affinity triggering in lymphocyte in vivo homing. Immunity 20, 25–35 (2004). · DOI
- Bos, J. L., de Rooij, J. & Reedquist, K. A. Rap1 signaling: adhering to new models. Nature Rev. Mol. Cell Biol. 2, 369–377 (2001). · DOI
- Sebzda, E., Bracke, M., Tugal, T., Hogg, N. & Cantrell, D. A. Rap1A positively regulates T cells via integrin activation rather than inhibiting lymphocyte signaling. Nature Immunol. 3, 251–258 (2002). · DOI
- Bertoni, A. et al. Relationships between Rap1b, affinity modulation of integrin αIIbβ3, and the actin cytoskeleton. J. Biol. Chem. 277, 25715–25721 (2002). · DOI
- Reedquist, K. A. et al. The small GTPase, Rap1, mediates CD31-induced integrin adhesion. J. Cell Biol. 148, 1151–1158 (2000). · DOI
- Tohyama, Y. et al. The critical cytoplasmic regions of the αL/β2 integrin in Rap1-induced adhesion and migration. Mol. Biol. Cell 14, 2570–2582 (2003). · DOI
- Hibbs, M. L., Jakes, S., Stacker, S. A., Wallace, R. W. & Springer, T. A. The cytoplasmic domain of the integrin lymphocyte-function-associated antigen 1 β subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site. J. Exp. Med. 174, 1227–1238 (1991). · DOI
- Hibbs, M. L., Xu, H., Stacker, S. A. & Springer, T. A. Regulation of adhesion to ICAM-1 by the cytoplasmic domain of LFA-1 integrin β subunit. Science 251, 1611–1613 (1991). · DOI
- Weber, C., Lu, C. -H., Casanovas, J. M. & Springer, T. A. Role of αLβ2 integrin avidity in transendothelial chemotaxis of mononuclear cells. J. Immunol. 159, 3968–3975 (1997). · DOI
- Shimonaka, M. et al. Rap1 translates chemokine signals to integrin activation, cell polarization, and motility across vascular endothelium under flow. J. Cell Biol. 161, 417–427 (2003). · DOI
- Kinashi, T. et al. LAD-III, a leukocyte adhesion deficiency syndrome associated with defective Rap1 activation and impaired stabilization of integrin bonds. Blood 103, 1033–1036 (2004). · DOI
- Alon, R. & Etzioni, A. LAD-III, a novel group of leukocyte integrin activation deficiencies. Trends Immunol. 24, 561–566 (2003). · DOI
- Katagiri, K., Maeda, A., Shimonaka, M. & Kinashi, T. RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1. Nature Immunol. 4, 741–748 (2003). This study identified RAPL as a RAP1 effector in lymphocytes that mediates LFA1- and VLA4-dependent adhesion, and it showed that RAP1–RAPL complexes coordinate affinity and valency regulation of LFA1. · DOI
- Tommasi, S. et al. RASSF3 and NORE1: identification and cloning of two human homologues of the putative tumor suppressor gene RASSF1. Oncogene 21, 2713–2720 (2002). · DOI
- Kinashi, T. & Katagiri, K. Regulation of lymphocyte adhesion and migration by the small GTPase Rap1 and its effector molecule, RAPL. Immunol. Lett. 93, 1–5 (2004). · DOI
- Katagiri, K. et al. Crucial roles of Rap1 effector molecule RAPL in lymphocyte and dendritic cell trafficking. Nature Immunol. 5, 1045–1051 (2004). Using gene targeting, this study showed that RAPL has an important role in the LFA1- and VLA4-dependent adhesion of lymphocytes stimulated with chemokines. · DOI
- Inagaki, T. et al. The retinoic acid-responsive proline-rich protein is identified in promyeloleukemic HL-60 cells. J. Biol. Chem. 278, 51685–51692 (2003). · DOI
- Jenzora, A., Behrendt, B., Small, J. V., Wehland, J. & Stradal, T. E. PREL1 provides a link from Ras signalling to the actin cytoskeleton via Ena/VASP proteins. FEBS Lett. 579, 455–463 (2005). · DOI
- Legg, J. A. & Machesky, L. M. MRL proteins: leading Ena/VASP to Ras GTPases. Nature Cell Biol. 6, 1015–1017 (2004). · DOI
- Sanui, T. et al. DOCK2 is essential for antigen-induced translocation of TCR and lipid rafts, but not PKC-θ and LFA-1, in T cells. Immunity 19, 119–129 (2003). · DOI
- Cherry, L. K., Li, X., Schwab, P., Lim, B. & Klickstein, L. B. RhoH is required to maintain the integrin LFA-1 in a nonadhesive state on lymphocytes. Nature Immunol. 5, 961–967 (2004). This was the first report that the weakly adhesive state of LFA1 is actively controlled by RHO-H. · DOI · Paper page
- Oinuma, I., Ishikawa, Y., Katoh, H. & Negishi, M. The semaphorin 4D receptor plexin-B1 is a GTPase activating protein for R-Ras. Science 305, 862–865 (2004). · DOI
- Zang, Z., Vuori, K., Wang, H. -G., Reed, J. C. & Ruoslahti, E. Integrin activation by R-ras. Cell 85, 61–69 (1996). · DOI
- Kinashi, T. et al. Distinct mechanisms of α5β1 integrin activation by Ha-Ras and R-Ras. J. Biol. Chem. 275, 22590–22596 (2000). · DOI
- Lucas, J. A., Miller, A. T., Atherly, L. O. & Berg, L. J. The role of Tec family kinases in T cell development and function. Immunol. Rev. 191, 119–138 (2003). · DOI
- Woods, M. L. et al. A novel function for the Tec family tyrosine kinase Itk in activation of β1 integrins by the T-cell receptor. EMBO J. 20, 1232–1244 (2001). · DOI
- Takesono, A., Horai, R., Mandai, M., Dombroski, D. & Schwartzberg, P. L. Requirement for Tec kinases in chemokine-induced migration and activation of Cdc42 and Rac. Curr. Biol. 14, 917–922 (2004). · DOI
- Labno, C. M. et al. Itk functions to control actin polymerization at the immune synapse through localized activation of Cdc42 and WASP. Curr. Biol. 13, 1619–1624 (2003). · DOI
- Fischer, A. M., Mercer, J. C., Iyer, A., Ragin, M. J. & August, A. Regulation of CXC chemokine receptor 4-mediated migration by the Tec family tyrosine kinase ITK. J. Biol. Chem. 279, 29816–29820 (2004). · DOI
- Kim, C. H. et al. Abnormal chemokine-induced responses of immature and mature hematopoietic cells from motheaten mice implicate the protein tyrosine phosphatase SHP-1 in chemokine responses. J. Exp. Med. 190, 681–690 (1999). · DOI
- Krawczyk, C. et al. Vav1 controls integrin clustering and MHC/peptide-specific cell adhesion to antigen-presenting cells. Immunity 16, 331–343 (2002). · DOI
- Tybulewicz, V. L., Ardouin, L., Prisco, A. & Reynolds, L. F. Vav1: a key signal transducer downstream of the TCR. Immunol. Rev. 192, 42–52 (2003). · DOI
- Peterson, E. J. et al. Coupling of the TCR to integrin activation by Slap-130/Fyb. Science 293, 2263–2265 (2001). · DOI
- Griffiths, E. K. et al. Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap. Science 293, 2260–2263 (2001). · DOI
- Peterson, E. J. The TCR ADAPts to integrin-mediated cell adhesion. Immunol. Rev. 192, 113–121 (2003). References 106 and 107 identified ADAP as a crucial mediator of activation of T-cell integrins after TCR ligation. · DOI
- Wang, H. et al. ADAP–SLP-76 binding differentially regulates supramolecular activation cluster (SMAC) formation relative to T cell–APC conjugation. J. Exp. Med. 200, 1063–1074 (2004). · DOI
- Wang, H. et al. SKAP-55 regulates integrin adhesion and formation of T cell–APC conjugates. Nature Immunol. 4, 366–374 (2003). · DOI
- Boussiotis, V. A., Freeman, G. J., Berezovskaya, A., Barber, D. L. & Nadler, L. M. Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap1. Science 278, 124–128 (1997). · DOI
- Katagiri, K., Hattori, M., Minato, N. & Kinashi, T. Rap1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses. Mol. Cell. Biol. 22, 1001–1015 (2002). · DOI
- Katagiri, K., Shimonaka, M. & Kinashi, T. Rap1-mediated LFA-1 activation by the T cell antigen receptor is dependent on PLC-γ1. J. Biol. Chem. 279, 11875–11881 (2004). · DOI
- McLeod, S. J. & Gold, M. R. Activation and function of the Rap1 GTPase in B lymphocytes. Int. Rev. Immunol. 20, 763–789 (2001). · DOI
- Amsen, D., Kruisbeek, A., Bos, J. L. & Reedquist, K. Activation of the Ras-related GTPase Rap1 by thymocyte TCR engagement and during selection. Eur. J. Immunol. 30, 2832–2841 (2000). · DOI
- Zhang, W. et al. Negative regulation of T cell antigen receptor-mediated Crk-L–C3G signaling and cell adhesion by Cbl-b. J. Biol. Chem. 278, 23978–23983 (2003). · DOI
- Samelson, L. E. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 20, 371–394 (2002). · DOI
- Kellermann, S. A., Dell, C. L., Hunt, S. W. & Shimizu, Y. Genetic analysis of integrin activation in T lymphocytes. Immunol. Rev. 186, 172–188 (2002). · DOI
- Reynolds, L. F. et al. Vav1 transduces T cell receptor signals to the activation of phospholipase C-γ1 via phosphoinositide 3-kinase-dependent and -independent pathways. J. Exp. Med. 195, 1103–1114 (2002). · DOI
- Fabbri, M. et al. A tyrosine-based sorting signal in the β2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand-supported migration. EMBO J. 18, 4915–4925 (1999). · DOI
- Bivona, T. G. et al. Rap1 up-regulation and activation on plasma membrane regulates T cell adhesion. J. Cell Biol. 164, 461–470 (2004). · DOI
- Worthylake, R. A., Lemoine, S., Watson, J. M. & Burridge, K. RhoA is required for monocyte tail retraction during transendothelial migration. J. Cell Biol. 154, 147–160 (2001). · DOI
- Smith, A., Bracke, M., Leitinger, B., Porter, J. C. & Hogg, N. LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment. J. Cell Sci. 116, 3123–3133 (2003). · DOI
- Lawson, M. A. & Maxfield, R. R. Ca2+- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils. Nature 377, 75–79 (1995). · DOI
- Martel, V. et al. Talin controls the exit of the integrin α5β1 from an early compartment of the secretory pathway. J. Cell Sci. 113, 1951–1961 (2000). · DOI
- Arthur, W. T., Quilliam, L. A. & Cooper, J. A. Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors. J. Cell Biol. 167, 111–122 (2004). · DOI
- Caloca, M. J., Zugaza, J. L., Vicente-Manzanares, M., Sanchez-Madrid, F. & Bustelo, X. R. F-actin-dependent translocation of the Rap1 GDP/GTP exchange factor RasGRP2. J. Biol. Chem. 279, 20435–20446 (2004). · DOI
- Song, M. S. et al. The tumour suppressor RASSF1A regulates mitosis by inhibiting the APC–Cdc20 complex. Nature Cell Biol. 6, 129–137 (2004). · DOI
- Fujita, H. et al. Local activation of Rap1 contributes to directional vascular endothelial cell migration accompanied by extension of microtubules on which RAPL, a Rap1-associating molecule, localizes. J. Biol. Chem. 280, 5022–5031 (2005). · DOI
- Kuhn, J. R. & Poenie, M. Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing. Immunity 16, 111–121 (2002). · DOI
Cited by
Getting to the site of inflammation: the leukocyte adhesion cascade updated
Ley, K., Laudanna, C., Cybulsky, M. I., & Nourshargh, S. (2007) · Nature Reviews Immunology · doi:10.1038/nri2156 · Cited by 4,354
Stewart, C. R., Stuart, L. M., Wilkinson, K., van Gils, J. M., Deng, J., Halle, A., Rayner, K. J., Boyer, L., Zhong, R., Frazier, W. A., et al. (2010) · Nature Immunology · doi:10.1038/ni.1836 · Cited by 1,513
Immune cell migration in inflammation: present and future therapeutic targets
Luster, A. D., Alon, R., & von Andrian, U. H. (2005) · Nature Immunology · doi:10.1038/ni1275 · Cited by 1,313
Role of β7 Integrins in Intestinal Lymphocyte Homing and Retention
Gorfu, G., Rivera-Nieves, J., & Ley, K. (2009) · Current Molecular Medicine · doi:10.2174/156652409789105525 · Cited by 292
Integrin modulation and signaling in leukocyte adhesion and migration
Rose, D. M., Alon, R., & Ginsberg, M. H. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00536.x · Cited by 243
Metadata
- Authors
- Kinashi, T.
- Venue
- Nature Reviews Immunology
- Published
- 2005-06-20
- Volume
- 5
- Issue
- 7
- Pages
- 546-559
- ISSN
- 1474-1733
- 1474-1741
- Cited by
- 477
- References
- 2
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Intracellular signalling controlling integrin activation in lymphocytes. https://app.cochat.ai/papers/10.1038/nri1646
- The paper
- Kinashi, T. (2005). Intracellular signalling controlling integrin activation in lymphocytes. Nature Reviews Immunology. https://doi.org/10.1038/nri1646