scholarly journals Faculty Opinions recommendation of Type-I myosins promote actin polymerization to drive membrane bending in endocytosis.

2021 ◽  
Author(s):  
Britta Qualmann
Keyword(s):  
Actin Polymerization ◽  
Type I ◽  
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 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

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 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.

scholarly journals Regulation of anaphylactic responses by phosphatidylinositol phosphate kinase type I α

2005 ◽  
Vol 201 (6) ◽  
pp. 859-870 ◽  
Author(s):  
Junko Sasaki ◽  
Takehiko Sasaki ◽  
Masakazu Yamazaki ◽  
Kunie Matsuoka ◽  
Choji Taya ◽  
...  
Keyword(s):  
Mast Cells ◽  
Actin Polymerization ◽  
Negative Regulator ◽  
Type I ◽  
Filamentous Actin ◽  
Critical Signal ◽  
Cell Functions ◽  
Phosphatidylinositol Phosphate

The membrane phospholipid phosphatidylinositol 4, 5-bisphosphate [PI(4,5)P2] is a critical signal transducer in eukaryotic cells. However, the physiological roles of the type I phosphatidylinositol phosphate kinases (PIPKIs) that synthesize PI(4,5)P2 are largely unknown. Here, we show that the α isozyme of PIPKI (PIPKIα) negatively regulates mast cell functions and anaphylactic responses. In vitro, PIPKIα-deficient mast cells exhibited increased degranulation and cytokine production after Fcε receptor-I cross-linking. In vivo, PIPKIα−/− mice displayed enhanced passive cutaneous and systemic anaphylaxis. Filamentous actin was diminished in PIPKIα−/− mast cells, and enhanced degranulation observed in the absence of PIPKIα was also seen in wild-type mast cells treated with latrunculin, a pharmacological inhibitor of actin polymerization. Moreover, the association of FcεRI with lipid rafts and FcεRI-mediated activation of signaling proteins was augmented in PIPKIα−/− mast cells. Thus, PIPKIα is a negative regulator of FcεRI-mediated cellular responses and anaphylaxis, which functions by controlling the actin cytoskeleton and dynamics of FcεRI signaling. Our results indicate that the different PIPKI isoforms might be functionally specialized.

scholarly journals Comparative mechanisms of cancer cell migration through 3D matrix and physiological microtracks

2015 ◽  
Vol 308 (6) ◽  
pp. C436-C447 ◽  
Author(s):  
Shawn P. Carey ◽  
Aniqua Rahman ◽  
Casey M. Kraning-Rush ◽  
Bethsabe Romero ◽  
Sahana Somasegar ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cancer Cell ◽  
Actin Polymerization ◽  
Cancer Metastasis ◽  
Type I Collagen ◽  
Type I ◽  
Cancer Cell Migration ◽  
Cytoskeletal Dynamics ◽  
3D Matrix ◽  
Context Specific

Tumor cell invasion through the stromal extracellular matrix (ECM) is a key feature of cancer metastasis, and understanding the cellular mechanisms of invasive migration is critical to the development of effective diagnostic and therapeutic strategies. Since cancer cell migration is highly adaptable to physiochemical properties of the ECM, it is critical to define these migration mechanisms in a context-specific manner. Although extensive work has characterized cancer cell migration in two- and three-dimensional (3D) matrix environments, the migration program employed by cells to move through native and cell-derived microtracks within the stromal ECM remains unclear. We previously reported the development of an in vitro model of patterned type I collagen microtracks that enable matrix metalloproteinase-independent microtrack migration. Here we show that collagen microtracks closely resemble channel-like gaps in native mammary stroma ECM and examine the extracellular and intracellular mechanisms underlying microtrack migration. Cell-matrix mechanocoupling, while critical for migration through 3D matrix, is not necessary for microtrack migration. Instead, cytoskeletal dynamics, including actin polymerization, cortical tension, and microtubule turnover, enable persistent, polarized migration through physiological microtracks. These results indicate that tumor cells employ context-specific mechanisms to migrate and suggest that selective targeting of cytoskeletal dynamics, but not adhesion, proteolysis, or cell traction forces, may effectively inhibit cancer cell migration through preformed matrix microtracks within the tumor stroma.

scholarly journals The PCH Family Member Proline-Serine-Threonine Phosphatase–interacting Protein 1 Targets to the Leukocyte Uropod and Regulates Directed Cell Migration

2008 ◽  
Vol 19 (8) ◽  
pp. 3180-3191 ◽  
Author(s):  
Kate M. Cooper ◽  
David A. Bennin ◽  
Anna Huttenlocher
Keyword(s):  
Cell Migration ◽  
Family Member ◽  
Actin Polymerization ◽  
Stable Population ◽  
Type I ◽  
Microtubule Network ◽  
Interacting Protein ◽  
Directed Cell Migration ◽  
Transferrin Uptake ◽  
Dynamin 2

Pombe Cdc15 homology (PCH) family members have emerged as important regulators of membrane–cytoskeletal interactions. Here we show that PSTPIP1, a PCH family member expressed in hematopoietic cells, regulates the motility of neutrophil-like cells and is a novel component of the leukocyte uropod where it colocalizes with other uropod components, such as type I PIPKIγ. Furthermore, we show that PSTPIP1 association with the regulator of endocytosis, dynamin 2, and PSTPIP1 expression impairs transferrin uptake and endocytosis. We also show that PSTPIP1 localizes at the rear of neutrophils with a subpopulation of F-actin that is specifically detected by the binding of an F-actin probe that detects a more stable population of actin. Finally, we show that actin polymerization, but not the microtubule network, is necessary for the polarized distribution of PSTPIP1 toward the rear of the cell. Together, our findings demonstrate that PSTPIP1 is a novel component of the leukocyte uropod that regulates endocytosis and cell migration.

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