Watts, C. & Marsh, M. Endocytosis: what goes in and how? J. Cell Sci.103, 1–8 (1992). PubMed Google Scholar
Watarai, M. et al. Legionella pneumophila is internalized by a macropinocytotic uptake pathway controlled by the Dot/Icm system and the mouse Lgn1 locus. J. Exp. Med.194, 1081–1096 (2001). CASPubMedPubMed Central Google Scholar
Francis, C. L., Ryan, T. A., Jones, B. D., Smith, S. J. & Falkow, S. Ruffles induced by Salmonella and other stimuli direct macropinocytosis of bacteria. Nature364, 639–642 (1993). CASPubMed Google Scholar
Fabbri, A. et al. Rho-activating Escherichia coli cytotoxic necrotizing factor 1: macropinocytosis of apoptotic bodies in human epithelial cells. Int. J. Med. Microbiol.291, 551–554 (2002). CASPubMed Google Scholar
Hoffmann, P. R. et al. Phosphatidylserine (PS) induces PS receptor-mediated macropinocytosis and promotes clearance of apoptotic cells. J. Cell Biol.155, 649–659 (2001). CASPubMedPubMed Central Google Scholar
Amyere, M. et al. Origin, originality, functions, subversions and molecular signalling of macropinocytosis. Int. J. Med. Microbiol.291, 487–494 (2002). CASPubMed Google Scholar
Donaldson, J. G., Porat-Shliom, N. & Cohen, L. A. Clathrin-independent endocytosis: a unique platform for cell signaling and PM remodeling. Cell. signal.21, 1–6 (2009). CASPubMed Google Scholar
Jones, A. T. Macropinocytosis: searching for an endocytic identity and role in the uptake of cell penetrating peptides. J. Cell. Mol. Med.11, 670–684 (2007). CASPubMedPubMed Central Google Scholar
Swanson, J. A. Shaping cups into phagosomes and macropinosomes. Nature Rev. Mol. Cell Biol.9, 639–649 (2008). CAS Google Scholar
Kirkham, M. & Parton, R. G. Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers. Biochim. Biophys. Acta.1746, 349–363 (2005). CASPubMed Google Scholar
Mayor, S. & Pagano, R. E. Pathways of clathrin-independent endocytosis. Nature Rev. Mol. Cell Biol.8, 603–612 (2007). CAS Google Scholar
Sansonetti, P. J. Microbes and microbial toxins: paradigms for microbial-mucosal interactions III. Shigellosis: from symptoms to molecular pathogenesis. Am. J. Phys.280, G319–323 (2001). CAS Google Scholar
Swanson, J. A. & Watts, C. Macropinocytosis. Trends Cell Biol.5, 424–428 (1995). CASPubMed Google Scholar
Swanson, J. A. Phorbol esters stimulate macropinocytosis and solute flow through macrophages. J. Cell Sci.94, 135–142 (1989). CASPubMed Google Scholar
Xu, W. et al. IL-10-producing macrophages preferentially clear early apoptotic cells. Blood107, 4930–4937 (2006). CASPubMed Google Scholar
Erwig, L. P. & Henson, P. M. Clearance of apoptotic cells by phagocytes. Cell Death Differ.15, 243–250 (2008). CASPubMed Google Scholar
Xiang, S. D. et al. Pathogen recognition and development of particulate vaccines: does size matter? Methods40, 1–9 (2006). CASPubMed Google Scholar
Maniak, M. Fluid-phase uptake and transit in axenic Dictyostelium cells. Biochim. Biophys. Acta.1525, 197–204 (2001). CASPubMed Google Scholar
Bar-Sagi, D., McCormick, F., Milley, R. J. & Feramisco, J. R. Inhibition of cell surface ruffling and fluid-phase pinocytosis by microinjection of anti-ras antibodies into living cells. J. Cell. Phys. 69–73 (1987).
Bar-Sagi, D. & Feramisco, J. R. Induction of membrane ruffling and fluid-phase pinocytosis in quiescent fibroblasts by ras proteins. Science233, 1061–1068 (1986). CASPubMed Google Scholar
Lanzetti, L., Palamidessi, A., Areces, L., Scita, G. & Di Fiore, P. P. Rab5 is a signalling GTPase involved in actin remodelling by receptor tyrosine kinases. Nature429, 309–314 (2004). CASPubMed Google Scholar
Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D. & Hall, A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell70, 401–410 (1992). CASPubMed Google Scholar
Mercer, J. & Helenius, A. Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science320, 531–535 (2008). CASPubMed Google Scholar
Garrett, W. S. et al. Developmental control of endocytosis in dendritic cells by Cdc42. Cell102, 325–334 (2000). CASPubMed Google Scholar
Chen, L. M., Hobbie, S. & Galan, J. E. Requirement of CDC42 for _Salmonella_-induced cytoskeletal and nuclear responses. Science274, 2115–2118 (1996). CASPubMed Google Scholar
Schnatwinkel, C. et al. The Rab5 effector Rabankyrin-5 regulates and coordinates different endocytic mechanisms. PLoS Biol.2, E261 (2004). PubMedPubMed Central Google Scholar
Donaldson, J. G. Arfs, phosphoinositides and membrane traffic. Biochem. Soc. Trans.33, 1276–1278 (2005). CASPubMed Google Scholar
Svensson, H. G. et al. A role for ARF6 in dendritic cell podosome formation and migration. Eur. J. Immunol.38, 818–828 (2008). CASPubMed Google Scholar
Lundmark, R., Doherty, G. J., Vallis, Y., Peter, B. J. & McMahon, H. T. Arf family GTP loading is activated by, and generates, positive membrane curvature. Biochem. J.414, 189–194 (2008). CASPubMed Google Scholar
Radhakrishna, H., Al-Awar, O., Khachikian, Z. & Donaldson, J. G. ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell Sci.112, 855–866 (1999). CASPubMed Google Scholar
Radhakrishna, H., Klausner, R. D. & Donaldson, J. G. Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase. J. Cell Biol.134, 935–947 (1996). CASPubMed Google Scholar
Porat-Shliom, N., Kloog, Y. & Donaldson, J. G. A unique platform for H-Ras signaling involving clathrin-independent endocytosis. Mol. Biol. Cell19, 765–775 (2008). CASPubMedPubMed Central Google Scholar
Franco, M. et al. EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization. EMBO J.18, 1480–1491 (1999). CASPubMedPubMed Central Google Scholar
Santy, L. C. & Casanova, J. E. Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D. J. Cell Biol.154, 599–610 (2001). CASPubMedPubMed Central Google Scholar
Liberali, P., Ramo, P. & Pelkmans, L. Protein kinases: starting a molecular systems view of endocytosis. Ann. Rev. Cell Dev. Biol.24, 501–523 (2008). CAS Google Scholar
Parrini, M. C., Matsuda, M. & de Gunzburg, J. Spatiotemporal regulation of the Pak1 kinase. Biochem. Soc. Trans.33, 646–648 (2005). CASPubMed Google Scholar
Dharmawardhane, S. et al. Regulation of macropinocytosis by p21-activated kinase-1. Mol. Biol. Cell11, 3341–3352 (2000). CASPubMedPubMed Central Google Scholar
Liberali, P. et al. The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS. EMBO J.27, 970–981 (2008). CASPubMedPubMed Central Google Scholar
Galisteo, M. L., Chernoff, J., Su, Y. C., Skolnik, E. Y. & Schlessinger, J. The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1. J. Biol. Chem.271, 20997–21000 (1996). CASPubMed Google Scholar
Puto, L. A., Pestonjamasp, K., King, C. C. & Bokoch, G. M. p21-activated kinase 1 (PAK1) interacts with the Grb2 adapter protein to couple to growth factor signaling. J. Biol. Chem.278, 9388–9393 (2003). CASPubMed Google Scholar
Dharmawardhane, S., Brownson, D., Lennartz, M. & Bokoch, G. M. Localization of p21-activated kinase 1 (PAK1) to pseudopodia, membrane ruffles, and phagocytic cups in activated human neutrophils. J. Leukoc. Biol.66, 521–527 (1999). CASPubMed Google Scholar
Dharmawardhane, S., Sanders, L. C., Martin, S. S., Daniels, R. H. & Bokoch, G. M. Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells. J. Cell Biol.138, 1265–1278 (1997). CASPubMedPubMed Central Google Scholar
Even-Faitelson, L., Rosenberg, M. & Ravid, S. PAK1 regulates myosin II-B phosphorylation, filament assembly, localization and cell chemotaxis. Cell. Signal.17, 1137–1148 (2005). CASPubMed Google Scholar
Sanders, L. C., Matsumura, F., Bokoch, G. M. & de Lanerolle, P. Inhibition of myosin light chain kinase by p21-activated kinase. Science283, 2083–2085 (1999). CASPubMed Google Scholar
Amyere, M. et al. Constitutive macropinocytosis in oncogene-transformed fibroblasts depends on sequential permanent activation of phosphoinositide 3-kinase and phospholipase C. Mol. Biol. Cell11, 3453–3467 (2000). CASPubMedPubMed Central Google Scholar
Miyata, Y., Nishida, E., Koyasu, S., Yahara, I. & Sakai, H. Protein kinase C-dependent and -independent pathways in the growth factor-induced cytoskeletal reorganization. J. Biol. Chem.264, 15565–15568 (1989). CASPubMed Google Scholar
Keller, H. U. Diacylglycerols and PMA are particularly effective stimulators of fluid pinocytosis in human neutrophils. J. Cell. Physiol.145, 465–471 (1990). CASPubMed Google Scholar
Kasahara, K. et al. Role of Src-family kinases in formation and trafficking of macropinosomes. J. Cell. Physiol.211, 220–232 (2007). CASPubMed Google Scholar
Sandilands, E. et al. RhoB and actin polymerization coordinate Src activation with endosome-mediated delivery to the membrane. Dev. Cell7, 855–869 (2004). CASPubMed Google Scholar
Donepudi, M. & Resh, M. D. c-Src trafficking and co-localization with the EGF receptor promotes EGF ligand-independent EGF receptor activation and signaling. Cell. Signal.20, 1359–1367 (2008). CASPubMedPubMed Central Google Scholar
Bougneres, L. et al. Cortactin and Crk cooperate to trigger actin polymerization during Shigella invasion of epithelial cells. J. Cell. Biol.166, 225–235 (2004). CASPubMedPubMed Central Google Scholar
West, M. A., Bretscher, M. S. & Watts, C. Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J. Cell. Biol.109, 2731–2739 (1989). CASPubMed Google Scholar
Dowrick, P., Kenworthy, P., McCann, B. & Warn, R. Circular ruffle formation and closure lead to macropinocytosis in hepatocyte growth factor/scatter factor-treated cells. Eur. J. Cell Biol.61, 44–53 (1993). CASPubMed Google Scholar
Ivanov, A. I. Pharmacological inhibition of endocytic pathways: is it specific enough to be useful? Methods Mol. Biol.440, 15–33 (2008). CASPubMed Google Scholar
Grimmer, S., van Deurs, B. & Sandvig, K. Membrane ruffling and macropinocytosis in A431 cells require cholesterol. J. Cell Sci.115, 2953–2962 (2002). CASPubMed Google Scholar
Kwik, J. et al. Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4, 5-bisphosphate-dependent organization of cell actin. Proc. Natl Acad. Sci. USA100, 13964–13969 (2003). CASPubMedPubMed Central Google Scholar
Charras, G. T., Hu, C. K., Coughlin, M. & Mitchison, T. J. Reassembly of contractile actin cortex in cell blebs. J. Cell Biol.175, 477–490 (2006). CASPubMedPubMed Central Google Scholar
Buccione, R., Orth, J. D. & McNiven, M. A. Foot and mouth: podosomes, invadopodia and circular dorsal ruffles. Nature Rev. Mol. Cell Biol.5, 647–657 (2004). CAS Google Scholar
Grogan, A. et al. Cytosolic phox proteins interact with and regulate the assembly of coronin in neutrophils. J. Cell Sci.110, 3071–3081 (1997). CASPubMed Google Scholar
Holt, M. R. & Koffer, A. Cell motility: proline-rich proteins promote protrusions. Trends Cell Biol.11, 38–46 (2001). CASPubMed Google Scholar
Suzuki, K. et al. Activation induces dephosphorylation of cofilin and its translocation to plasma membranes in neutrophil-like differentiated HL-60 cells. J. Biol. Chem.270, 19551–19556 (1995). CASPubMed Google Scholar
Lavoie, J. N., Hickey, E., Weber, L. A. & Landry, J. Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J. Biol. Chem.268, 24210–24214 (1993). CASPubMed Google Scholar
Bretscher, A., Reczek, D. & Berryman, M. Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J. Cell Sci.110, 3011–3018 (1997). CASPubMed Google Scholar
D'Angelo, R. et al. Interaction of ezrin with the novel guanine nucleotide exchange factor PLEKHG6 promotes RhoG-dependent apical cytoskeleton rearrangements in epithelial cells. Mol. Biol. Cell18, 4780–4793 (2007). CASPubMedPubMed Central Google Scholar
Machesky, L. M. et al. Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins. Biochem. J.328, 105–112 (1997). CASPubMedPubMed Central Google Scholar
Takenawa, T. & Suetsugu, S. The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nature Rev. Mol. Cell Biol.8, 37–48 (2007). CAS Google Scholar
Pollard, T. D. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct.36, 451–477 (2007). CASPubMed Google Scholar
Sun, P. et al. Small GTPase Rah/Rab34 is associated with membrane ruffles and macropinosomes and promotes macropinosome formation. J. Biol. Chem.278, 4063–4071 (2003). CASPubMed Google Scholar
Goldenberg, N. M., Grinstein, S. & Silverman, M. Golgi-bound Rab34 is a novel member of the secretory pathway. Mol. Biol. Cell18, 4762–4771 (2007). CASPubMedPubMed Central Google Scholar
Lindmo, K. & Stenmark, H. Regulation of membrane traffic by phosphoinositide 3-kinases. J.Cell Sci.119, 605–614 (2006). CASPubMed Google Scholar
Araki, N., Egami, Y., Watanabe, Y. & Hatae, T. Phosphoinositide metabolism during membrane ruffling and macropinosome formation in EGF-stimulated A431 cells. Exp. Cell Res.313, 1496–1507 (2007). CASPubMed Google Scholar
Hawkins, P. T. et al. PDGF stimulates an increase in GTP-Rac via activation of phosphoinositide 3-kinase. Curr. Biol.5, 393–403 (1995). CASPubMed Google Scholar
Araki, N., Johnson, M. T. & Swanson, J. A. A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J. Cell Biol.135, 1249–1260 (1996). CASPubMed Google Scholar
Araki, N., Hamasaki, M., Egami, Y. & Hatae, T. Effect of 3-methyladenine on the fusion process of macropinosomes in EGF-stimulated A431 cells. Cell Struct. Funct.31, 145–157 (2006). CASPubMed Google Scholar
Buss, F. et al. The localization of myosin VI at the golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation. J. Cell Biol.143, 1535–1545 (1998). CASPubMedPubMed Central Google Scholar
Chew, T. L., Masaracchia, R. A., Goeckeler, Z. M. & Wysolmerski, R. B. Phosphorylation of non-muscle myosin II regulatory light chain by p21-activated kinase (γ-PAK). J. Muscle Res. Cell Motil.19, 839–854 (1998). CASPubMed Google Scholar
Araki, N., Hatae, T., Furukawa, A. & Swanson, J. A. Phosphoinositide-3-kinase-independent contractile activities associated with Fcγ-receptor-mediated phagocytosis and macropinocytosis in macrophages. J. Cell Sci.116, 247–257 (2003). CASPubMed Google Scholar
Swanson, J. A. et al. A contractile activity that closes phagosomes in macrophages. J. Cell Sci.112, 307–316 (1999). CASPubMed Google Scholar
Liu, Y. W., Surka, M. C., Schroeter, T., Lukiyanchuk, V. & Schmid, S. L. Isoform and splice-variant specific functions of dynamin-2 revealed by analysis of conditional knock-out cells. Mol. Biol. Cell19, 5347–5359 (2008). CASPubMedPubMed Central Google Scholar
Cao, H., Chen, J., Awoniyi, M., Henley, J. R. & McNiven, M. A. Dynamin 2 mediates fluid-phase micropinocytosis in epithelial cells. J. Cell Sci.120, 4167–4177 (2007). CASPubMed Google Scholar
Hewlett, L. J., Prescott, A. R. & Watts, C. The coated pit and macropinocytic pathways serve distinct endosome populations. J. Cell Biol.124, 689–703 (1994). CASPubMed Google Scholar
Racoosin, E. L. & Swanson, J. A. Macropinosome maturation and fusion with tubular lysosomes in macrophages. J. Cell Biol.121, 1011–1020 (1993). CASPubMed Google Scholar
Roberts, R. L., Barbieri, M. A., Ullrich, J. & Stahl, P. D. Dynamics of rab5 activation in endocytosis and phagocytosis. J. Leukoc. Biol.68, 627–632 (2000). CASPubMed Google Scholar
Hamasaki, M., Araki, N. & Hatae, T. Association of early endosomal autoantigen 1 with macropinocytosis in EGF-stimulated A431 cells. Anat. Rec.277, 298–306 (2004). Google Scholar
Kerr, M. C. et al. Visualisation of macropinosome maturation by the recruitment of sorting nexins. J. Cell Sci.119, 3967–3980 (2006). CASPubMed Google Scholar
Lim, J. P., Wang, J. T., Kerr, M. C., Teasdale, R. D. & Gleeson, P. A. A role for SNX5 in the regulation of macropinocytosis. BMC Cell Biol.9, 58 (2008). PubMedPubMed Central Google Scholar
Bryant, D. M. et al. EGF induces macropinocytosis and SNX1-modulated recycling of E-cadherin. J. Cell Sci.120, 1818–1828 (2007). CASPubMed Google Scholar
Merino-Trigo, A. et al. Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation. J. Cell Sci.117, 6413–6424 (2004). CASPubMed Google Scholar
Pelkmans, L. et al. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature436, 78–86 (2005). CASPubMed Google Scholar
Locker, J. K. et al. Entry of the two infectious forms of vaccinia virus at the plasma membane is signaling-dependent for the IMV but not the EEV. Mol. Biol. Cell11, 2497–2511 (2000). CASPubMedPubMed Central Google Scholar
Huang, C. Y. et al. A novel cellular protein, VPEF, facilitates vaccinia virus penetration into HeLa cells through fluid phase endocytosis. J. Virol.82, 7988–7999 (2008). CASPubMedPubMed Central Google Scholar
Townsley, A. C., Weisberg, A. S., Wagenaar, T. R. & Moss, B. Vaccinia virus entry into cells via a low-pH-dependent endosomal pathway. J. Virol.80, 8899–8908 (2006). CASPubMedPubMed Central Google Scholar
Chung, C. S., Huang, C. Y. & Chang, W. Vaccinia virus penetration requires cholesterol and results in specific viral envelope proteins associated with lipid rafts. J. Virol.79, 1623–1634 (2005). CASPubMedPubMed Central Google Scholar
Ichihashi, Y. & Oie, M. The activation of vaccinia virus infectivity by the transfer of phosphatidylserine from the plasma membrane. Virology130, 306–317 (1983). CASPubMed Google Scholar
Henson, P. M., Bratton, D. L. & Fadok, V. A. Apoptotic cell removal. Curr. Biol.11, R795–805 (2001). CASPubMed Google Scholar
Lucas, M. et al. Correlative 3D Microscopy: CLSM and FIB/SEM tomography. A study of cellular entry of vaccinia virus. Imaging Microsc.10, 30–31 (2008). Google Scholar
Niebuhr, K. et al. Conversion of PtdIns(4, 5)P(2) into PtdIns(5)P by the S.flexneri effector IpgD reorganizes host cell morphology. EMBO J.21, 5069–5078 (2002). CASPubMedPubMed Central Google Scholar
Young, V. B., Falkow, S. & Schoolnik, G. K. The invasin protein of Yersinia enterocolitica: internalization of invasin-bearing bacteria by eukaryotic cells is associated with reorganization of the cytoskeleton. J. Cell Biol.116, 197–207 (1992). CASPubMed Google Scholar
Amstutz, B. et al. Subversion of CtBP1-controlled macropinocytosis by human adenovirus serotype 3. EMBO J.27, 956–969 (2008). CASPubMedPubMed Central Google Scholar
Sirena, D. et al. The human membrane cofactor CD46 is a receptor for species B adenovirus serotype 3. J. Virol.78, 4454–4462 (2004). CASPubMedPubMed Central Google Scholar
Wickham, T. J., Mathias, P., Cheresh, D. A. & Nemerow, G. R. Integrins α v β 3 and α v β 5 promote adenovirus internalization but not virus attachment. Cell73, 309–319 (1993). CASPubMed Google Scholar
Karjalainen, M. et al. A Raft-derived, Pak1-regulated entry participates in α2β1 integrin-dependent sorting to caveosomes. Mol. Biol. Cell19, 2857–2869 (2008). CASPubMedPubMed Central Google Scholar
Coyne, C. B., Shen, L., Turner, J. R. & Bergelson, J. M. Coxsackievirus entry across epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5. Cell Host Microbe2, 181–192 (2007). CASPubMedPubMed Central Google Scholar
Coyne, C. B. & Bergelson, J. M. Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions. Cell124, 119–131 (2006). CASPubMed Google Scholar
Shukla, D. & Spear, P. G. Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry. J. Clin. Invest.108, 503–510 (2001). CASPubMedPubMed Central Google Scholar
Garner, J. A. Herpes simplex virion entry into and intracellular transport within mammalian cells. Adv. Drug Deliv. Rev.55, 1497–1513 (2003). CASPubMed Google Scholar
Nicola, A. V., Hou, J., Major, E. O. & Straus, S. E. Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway. J. Virol.79, 7609–7616 (2005). CASPubMedPubMed Central Google Scholar
Nicola, A. V., McEvoy, A. M. & Straus, S. E. Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells. J. Virol.77, 5324–5332 (2003). CASPubMedPubMed Central Google Scholar
Marechal, V. et al. Human immunodeficiency virus type 1 entry into macrophages mediated by macropinocytosis. J. Virol.75, 11166–11177 (2001). CASPubMedPubMed Central Google Scholar
Liu, N. Q. et al. Human immunodeficiency virus type 1 enters brain microvascular endothelia by macropinocytosis dependent on lipid rafts and the mitogen-activated protein kinase signaling pathway. J. Virol.76, 6689–6700 (2002). CASPubMedPubMed Central Google Scholar
Wang, J. H., Wells, C. & Wu, L. Macropinocytosis and cytoskeleton contribute to dendritic cell-mediated HIV-1 transmission to CD4+ T cells. Virology381, 143–154 (2008). CASPubMed Google Scholar
Nguyen, D. G., Wolff, K. C., Yin, H., Caldwell, J. S. & Kuhen, K. L. “UnPAKing” human immunodeficiency virus (HIV) replication: using small interfering RNA screening to identify novel cofactors and elucidate the role of group I PAKs in HIV infection. J. Virol.80, 130–137 (2006). CASPubMedPubMed Central Google Scholar
Fontenot, D. R. et al. Dynein light chain 1 peptide inhibits human immunodeficiency virus infection in eukaryotic cells. Biochem. Biophys. Res.Commun.363, 901–907 (2007). CASPubMed Google Scholar
Meier, O. et al. Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake. J. Cell Biol.158, 1119–1131 (2002). CASPubMedPubMed Central Google Scholar
Imelli, N., Meier, O., Boucke, K., Hemmi, S. & Greber, U. F. Cholesterol is required for endocytosis and endosomal escape of adenovirus type 2. J. Virol.78, 3089–3098 (2004). CASPubMedPubMed Central Google Scholar
Meier, O. & Greber, U. F. Adenovirus endocytosis. J. Gene Med.5, 451–462 (2003). CASPubMed Google Scholar
Lee, J. Y. & Bowden, D. S. Rubella virus replication and links to teratogenicity. Clin. Microbiol. Rev.13, 571–587 (2000). CASPubMedPubMed Central Google Scholar
Kee, S. H. et al. Effects of endocytosis inhibitory drugs on rubella virus entry into VeroE6 cells. Microbiol. Immunol.48, 823–829 (2004). CASPubMed Google Scholar
Petruzziello, R. et al. Pathway of rubella virus infectious entry into Vero cells. J. Gen. Virol.77, 303–308 (1996). CASPubMed Google Scholar
Albert, M. L. Death-defying immunity: do apoptotic cells influence antigen processing and presentation? Nat Rev Immunol4, 223–231 (2004). CASPubMed Google Scholar
Hayasaka, D., Ennis, F. A. & Terajima, M. Pathogeneses of respiratory infections with virulent and attenuated vaccinia viruses. Virol. J.4, 22 (2007). PubMedPubMed Central Google Scholar
Araki, N., Hatae, T., Yamada, T. & Hirohashi, S. Actinin-4 is preferentially involved in circular ruffling and macropinocytosis in mouse macrophages: analysis by fluorescence ratio imaging. J. Cell Sci.113, 3329–3340 (2000). CASPubMed Google Scholar
Deacon, S. W. et al. An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase. Chem. Biol.15, 322–331 (2008). CASPubMedPubMed Central Google Scholar