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Related Concept Videos

Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well characterized.
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Role of Myosin in Cell Migration01:18

Role of Myosin in Cell Migration

Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
Myosin II  is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction. It is...
Membrane Lipids01:32

Membrane Lipids

Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...

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Myo1e/f regulate phagocytic podosomes to promote efficient cup closure in macrophages.

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A local solution to local load: Myo1E as a tension-responsive actuator in clathrin-mediated endocytosis.

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Related Experiment Video

Updated: Jun 8, 2026

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
10:31

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2

Published on: September 26, 2025

Myo1e binds anionic phospholipids with high affinity.

Elizabeth A Feeser1, Cherry Mae G Ignacio, Mira Krendel

  • 1Pennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

Biochemistry
|September 24, 2010
PubMed
Summary

Myo1e protein binds tightly to anionic phospholipids in cell membranes. This interaction is primarily driven by electrostatic forces, not specific lipid recognition, influencing its cellular functions.

More Related Videos

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Related Experiment Videos

Last Updated: Jun 8, 2026

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
10:31

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2

Published on: September 26, 2025

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Area of Science:

  • Molecular and Cellular Biology
  • Biochemistry
  • Membrane Biology

Background:

  • Myo1e is a motor protein involved in cellular processes like endocytosis and kidney podocyte function.
  • Its C-terminal tail contains a basic region for vesicle localization and a pleckstrin-homology (PH) domain implicated in phospholipid binding.

Purpose of the Study:

  • To investigate the membrane binding properties of the Myo1e C-terminal tail.
  • To determine the binding affinities, kinetics, and in vivo localization mechanisms of Myo1e tail constructs.

Main Methods:

  • Sedimentation assays to measure binding affinity.
  • Stopped-flow fluorescence to analyze binding and dissociation kinetics.
  • Fluorescence microscopy for in vivo localization studies.

Main Results:

  • The Myo1e tail exhibits strong binding to anionic phospholipids like phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)) and phosphatidylserine.
  • Myo1e attachment to membranes is rapid, nearing the diffusion limit, with slow dissociation rates.
  • Mutations in the PH domain minimally impacted in vitro lipid binding or in vivo membrane localization.

Conclusions:

  • Myo1e interacts with lipids via non-specific electrostatic interactions rather than stereospecific phosphoinositide recognition.
  • Soluble inositol phosphates can compete for binding but with significantly lower affinity than membrane-bound PtdIns(4,5)P(2).