Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Myosin I

L M Coluccio1

  • 1Boston Biomedical Research Institute, Massachusetts 02114, USA.

The American Journal of Physiology
|August 1, 1997
PubMed
Summary
This summary is machine-generated.

Class I myosins are single-headed motor proteins. Research reviews their properties and proposed roles in intracellular trafficking and membrane structure changes.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Nanometre resolution tracking of myosin-1b motility.

IEE proceedings. Nanobiotechnology·2006
Same author

Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding.

The Journal of biological chemistry·2000
Same author

Truncation of a mammalian myosin I results in loss of Ca2+-sensitive motility.

The Journal of biological chemistry·2000
Same author

The XXVIII European Muscle conference. York, UK, 4-7 September 1999.

Journal of muscle research and cell motility·2000
Same author

Brush border myosin I (BBMI): a basally localized transcript in human jejunal enterocytes.

The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society·2000
Same author

Overlapping distribution of the 130- and 110-kDa myosin I isoforms on rat liver membranes.

Archives of biochemistry and biophysics·1999
Same journal

Blood coagulation in fish.

The American journal of physiology·2011
Same journal

Renal tubular reabsorption, metabolic utilization and isomeric fractionation of lactic acid in the dog.

The American journal of physiology·2010
Same journal

The inactivation of placental toxin by human serum.

The American journal of physiology·2010
Same journal

Adrenal function following ovariectomy in the rat.

The American journal of physiology·2010
Same journal

Capillary permeability; perfusion of frog and guinea pig hind limbs.

The American journal of physiology·2010
Same journal

Evaluation of protective measures against sunburn.

The American journal of physiology·2010
See all related articles

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Class I myosins are single-headed, actin-binding mechanochemical motor proteins.
  • They are composed of heavy chains (110-130 kDa) and associated light chains, often calmodulin in vertebrates, which may regulate motor activity.
  • Myosin I isoforms are found across eukaryotes and exhibit variations in regulation, such as phosphorylation in lower eukaryotes.

Purpose of the Study:

  • To review the current understanding of Class I myosin properties.
  • To discuss the proposed roles of Class I myosins in cellular functions.
  • To explore the structural and regulatory diversity among myosin I subclasses.

Main Methods:

  • Sequence analyses of amino-terminal head domains to classify myosin I subclasses.

Related Experiment Videos

  • Biochemical characterization of isolated myosin I molecules.
  • Cellular localization studies to infer functional roles.

    • Main Results:

    • Class I myosins are structurally distinct from other myosin classes, lacking filament formation.
    • Sequence analysis reveals distinct subclasses within myosin I.
    • Biochemical and localization data support roles in intracellular trafficking and membrane dynamics.

    Conclusions:

    • Class I myosins are versatile motor proteins with diverse roles in cellular processes.
    • Understanding their subclasses and regulatory mechanisms is crucial for elucidating their functions.
    • Further research is needed to fully define the contributions of myosin I to membrane dynamics and transport.