scholarly journals Author response: Type-I myosins promote actin polymerization to drive membrane bending in endocytosis

2019 ◽  
Author(s):  
Hetty E Manenschijn ◽  
Andrea Picco ◽  
Markus Mund ◽  
Anne-Sophie Rivier-Cordey ◽  
Jonas Ries ◽  
...  
Keyword(s):  
Actin Polymerization ◽  
Author Response ◽  
Type I ◽  
Response Type ◽  
Membrane Bending

scholarly journals Type-I myosins promote actin polymerization to drive membrane bending in endocytosis

2018 ◽  
Author(s):  
Hetty E Manenschijn ◽  
Andrea Picco ◽  
Markus Mund ◽  
Jonas Ries ◽  
Marko Kaksonen
Keyword(s):  
Live Cell Imaging ◽  
Actin Polymerization ◽  
Cell Imaging ◽  
Turgor Pressure ◽  
Type I ◽  
Actin Network ◽  
Actin Nucleation ◽  
Genetic Perturbations ◽  
Membrane Bending ◽  
Dose Dependent

Clathrin-mediated endocytosis in budding yeast requires the formation of a dynamic actin network that produces the force to invaginate the plasma membrane against the intracellular turgor pressure. The type-I myosins Myo3 and Myo5 are important for endocytic membrane reshaping, but mechanistic details of their function remain scarce. Here, we studied the function of Myo3 and Myo5 during endocytosis using quantitative live-cell imaging and genetic perturbations. We show that the type-I myosins promote, in a dose-dependent way, the growth and expansion of the actin network, which controls the speed of membrane and coat internalization. We found that this myosin-activity is independent of the actin nucleation promoting activity of myosins, and cannot be compensated for by increasing actin nucleation. Our results suggest a new mechanism for type-I myosins to produce force by promoting actin filament polymerization.

scholarly journals Author response: Type I interferon underlies severe disease associated with Junín virus infection in mice

2020 ◽  
Author(s):  
Brady T Hickerson ◽  
Eric J Sefing ◽  
Kevin W Bailey ◽  
Arnaud J Van Wettere ◽  
Manuel L Penichet ◽  
...  
Keyword(s):  
Virus Infection ◽  
Type I Interferon ◽  
Severe Disease ◽  
Author Response ◽  
Type I ◽  
Response Type ◽  
Junin Virus ◽  
Junín Virus

scholarly journals Type-I myosins promote actin polymerization to drive membrane bending in endocytosis

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Hetty E Manenschijn ◽  
Andrea Picco ◽  
Markus Mund ◽  
Anne-Sophie Rivier-Cordey ◽  
Jonas Ries ◽  
...  
Keyword(s):  
Live Cell Imaging ◽  
Actin Polymerization ◽  
Cell Imaging ◽  
Turgor Pressure ◽  
Type I ◽  
Actin Network ◽  
Actin Nucleation ◽  
Genetic Perturbations ◽  
Membrane Bending ◽  
Dose Dependent

Clathrin-mediated endocytosis in budding yeast requires the formation of a dynamic actin network that produces the force to invaginate the plasma membrane against the intracellular turgor pressure. The type-I myosins Myo3 and Myo5 are important for endocytic membrane reshaping, but mechanistic details of their function remain scarce. Here, we studied the function of Myo3 and Myo5 during endocytosis using quantitative live-cell imaging and genetic perturbations. We show that the type-I myosins promote, in a dose-dependent way, the growth and expansion of the actin network, which controls the speed of membrane and coat internalization. We found that this myosin-activity is independent of the actin nucleation promoting activity of myosins, and cannot be compensated for by increasing actin nucleation. Our results suggest a new mechanism for type-I myosins to produce force by promoting actin filament polymerization.

scholarly journals Author response: Type III CRISPR-Cas systems can provide redundancy to counteract viral escape from type I systems

2017 ◽  
Author(s):  
Sukrit Silas ◽  
Patricia Lucas-Elio ◽  
Simon A Jackson ◽  
Alejandra Aroca-Crevillén ◽  
Loren L Hansen ◽  
...  
Keyword(s):  
Viral Escape ◽  
Author Response ◽  
Type I ◽  
Response Type ◽  
Type Iii

Author response for "Type I interferons provide additive signals for murine regulatory B cell induction by Schistosoma mansoni eggs"

2018 ◽  
Author(s):  
Katja Obieglo ◽  
Alice Costain ◽  
Lauren M. Webb ◽  
Arifa Ozir‐Fazalalikhan ◽  
Shelia L. Brown ◽  
...  
Keyword(s):  
B Cell ◽  
Type I Interferons ◽  
Author Response ◽  
Type I ◽  
Regulatory B Cell ◽  
Cell Induction

scholarly journals Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis

2012 ◽  
Vol 23 (15) ◽  
pp. 2891-2904 ◽  
Author(s):  
Jackie Cheng ◽  
Alexandre Grassart ◽  
David G. Drubin
Keyword(s):  
Mammalian Cells ◽  
Actin Polymerization ◽  
Type I ◽  
Actin Assembly ◽  
Significant Delay ◽  
Src Homology 3 ◽  
Integral Role ◽  
Src Homology 3 Domain ◽  
Src Homology ◽  
Endocytic Vesicles

Myosin 1E (Myo1E) is recruited to sites of clathrin-mediated endocytosis coincident with a burst of actin assembly. The recruitment dynamics and lifetime of Myo1E are similar to those of tagged actin polymerization regulatory proteins. Like inhibition of actin assembly, depletion of Myo1E causes reduced transferrin endocytosis and a significant delay in transferrin trafficking to perinuclear compartments, demonstrating an integral role for Myo1E in these actin-mediated steps. Mistargeting of GFP-Myo1E or its src-homology 3 domain to mitochondria results in appearance of WIP, WIRE, N-WASP, and actin filaments at the mitochondria, providing evidence for Myo1E's role in actin assembly regulation. These results suggest for mammalian cells, similar to budding yeast, interdependence in the recruitment of type I myosins, WIP/WIRE, and N-WASP to endocytic sites for Arp2/3 complex activation to assemble F-actin as endocytic vesicles are being formed.

scholarly journals Type I phosphatidylinositol 4-phosphate 5-kinase controls neutrophil polarity and directional movement

2007 ◽  
Vol 179 (7) ◽  
pp. 1539-1553 ◽  
Author(s):  
Rosa Ana Lacalle ◽  
Rosa M. Peregil ◽  
Juan Pablo Albar ◽  
Ernesto Merino ◽  
Carlos Martínez-A ◽  
...  
Keyword(s):  
Actin Polymerization ◽  
Cell Movement ◽  
Leading Edge ◽  
Cell Polarization ◽  
Type I ◽  
Lipid Kinase ◽  
Erm Proteins ◽  
Chemical Gradients ◽  
C Terminus ◽  
Phosphatidylinositol 4

Directional cell movement in response to external chemical gradients requires establishment of front–rear asymmetry, which distinguishes an up-gradient protrusive leading edge, where Rac-induced F-actin polymerization takes place, and a down-gradient retractile tail (uropod in leukocytes), where RhoA-mediated actomyosin contraction occurs. The signals that govern this spatial and functional asymmetry are not entirely understood. We show that the human type I phosphatidylinositol 4-phosphate 5-kinase isoform β (PIPKIβ) has a role in organizing signaling at the cell rear. We found that PIPKIβ polarized at the uropod of neutrophil-differentiated HL60 cells. PIPKIβ localization was independent of its lipid kinase activity, but required the 83 C-terminal amino acids, which are not homologous to other PIPKI isoforms. The PIPKIβ C terminus interacted with EBP50 (4.1-ezrin-radixin-moesin (ERM)-binding phosphoprotein 50), which enabled further interactions with ERM proteins and the Rho-GDP dissociation inhibitor (RhoGDI). Knockdown of PIPKIβ with siRNA inhibited cell polarization and impaired cell directionality during dHL60 chemotaxis, suggesting a role for PIPKIβ in these processes.

scholarly journals Interaction of the Endocytic Scaffold Protein Pan1 with the Type I Myosins Contributes to the Late Stages of Endocytosis

2007 ◽  
Vol 18 (8) ◽  
pp. 2893-2903 ◽  
Author(s):  
Sarah L. Barker ◽  
Linda Lee ◽  
B. Daniel Pierce ◽  
Lymarie Maldonado-Báez ◽  
David G. Drubin ◽  
...  
Keyword(s):  
Late Stage ◽  
Actin Polymerization ◽  
Fluorescent Protein ◽  
Temperature Sensitive ◽  
Type I ◽  
Reading Frame ◽  
Rich Domain ◽  
C Terminus

The yeast endocytic scaffold Pan1 contains an uncharacterized proline-rich domain (PRD) at its carboxy (C)-terminus. We report that the pan1-20 temperature-sensitive allele has a disrupted PRD due to a frame-shift mutation in the open reading frame of the domain. To reveal redundantly masked functions of the PRD, synthetic genetic array screens with a pan1ΔPRD strain found genetic interactions with alleles of ACT1, LAS17 and a deletion of SLA1. Through a yeast two-hybrid screen, the Src homology 3 domains of the type I myosins, Myo3 and Myo5, were identified as binding partners for the C-terminus of Pan1. In vitro and in vivo assays validated this interaction. The relative timing of recruitment of Pan1-green fluorescent protein (GFP) and Myo3/5-red fluorescent protein (RFP) at nascent endocytic sites was revealed by two-color real-time fluorescence microscopy; the type I myosins join Pan1 at cortical patches at a late stage of internalization, preceding the inward movement of Pan1 and its disassembly. In cells lacking the Pan1 PRD, we observed an increased lifetime of Myo5-GFP at the cortex. Finally, Pan1 PRD enhanced the actin polymerization activity of Myo5–Vrp1 complexes in vitro. We propose that Pan1 and the type I myosins interactions promote an actin activity important at a late stage in endocytic internalization.

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