ArticleMolecular biology of the cell2017
Adhesion force and attachment lifetime of the KIF16B-PX domain interaction with lipid membranes.
Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- KIF16B drives MT1-MMP recycling in macrophages and promotes co-invasion of cancer cells.Life science alliance · 2023Article
- Choreographing the motor-driven endosomal dance.Journal of cell science · 2023Review
- Transcription factor EB regulates phosphatidylinositol-3-phosphate levels that control lysosome positioning in the bladder cancer model.Communications biology · 2023Article
- Is There a Need for a More Precise Description of Biomolecule Interactions to Understand Cell Function?Current issues in molecular biology · 2022Review
- Article
- Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment.Frontiers in cell and developmental biology · 2021Article
- Spatial control of membrane traffic in neuronal dendrites.Molecular and cellular neurosciences · 2020Review
- PX Domain-Containing Kinesin KIF16B and Microtubule-Dependent Intracellular Movements.The Journal of membrane biology · 2020Review
- Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting.Nature communications · 2019Article
- Mechanisms of lysosomal positioning and movement.Traffic (Copenhagen, Denmark) · 2018Review
- The Role of Glycans in Bacterial Adhesion to Mucosal Surfaces: How Can Single-Molecule Techniques Advance Our Understanding?Microorganisms · 2018Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
KIF16B is a highly processive kinesin-3 family member that participates in the trafficking and tubulation of early endosomes along microtubules. KIF16B attaches to lipid cargoes via a PX motif at its C-terminus, which has nanomolar affinity for bilayers containing phosphatidylinositol-3-phosphate (PI[3]P). As the PX domain has been proposed to be a primary mechanical anchor for the KIF16B-cargo attachment, we measured the adhesion forces and detachment kinetics of the PX domain as it interacts with membranes containing 2% PI(3)P and 98% phosphatidylcholine. Using optical tweezers, we found that the adhesion strength of a single PX domain ranged between 19 and 54 pN at loading rates between 80 and 1500 pN/s. These forces are substantially larger than the interaction of the adhesion of a pleckstrin homology domain with phosphatidylinositol 4,5-bisphosphate. This increased adhesion is the result of the membrane insertion of hydrophobic residues adjacent to the PI(3)P binding site, in addition to electrostatic interactions with PI(3)P. Attachment lifetimes under load decrease monotonically with force, indicating slip-bond behavior. However, the lifetime of membrane attachment under load appears to be well matched to the duration of processive motility of the KIF16B motor, indicating the PX domain is a suitable mechanical anchor for intracellular transport.
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