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

Spectrin and related molecules.

S R Goodman1, K E Krebs, C F Whitfield

  • 1Cell and Molecular Biology Center, Milton S. Hershey Medical Center, Pennsylvania State University.

CRC Critical Reviews in Biochemistry
|January 1, 1988
PubMed
Summary
This summary is machine-generated.

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

Standard operating procedures in experimental liver research: time to achieve uniformity.

Laboratory animals·2015
Same author

An equilibrium-point model of electromyographic patterns during single-joint movements based on experimentally reconstructed control signals.

Journal of electromyography and kinesiology : official journal of the International Society of Electrophysiological Kinesiology·2010
Same author

Topical application of naltrexone facilitates reepithelialization of the cornea in diabetic rabbits.

Brain research bulletin·2009
Same author

Phosphorylation of neurofilament subunit NF-M is regulated by activation of NMDA receptors and modulates cytoskeleton stability and neuronal shape.

Cell motility and the cytoskeleton·2008
Same author

Phosphorylation-dependent dimerization and subcellular localization of islet-brain 1/c-Jun N-terminal kinase-interacting protein 1.

Journal of neuroscience research·2007
Same author

Characterization of MAP1B heavy chain interaction with actin.

Brain research bulletin·2007
Same journal

DNA strand exchanges.

CRC critical reviews in biochemistry·1988
Same journal

Methionine biosynthesis in Enterobacteriaceae: biochemical, regulatory, and evolutionary aspects.

CRC critical reviews in biochemistry·1988
Same journal

Viral RNA polymerases.

CRC critical reviews in biochemistry·1988
Same journal

Positional isotope exchange.

CRC critical reviews in biochemistry·1988
Same journal

Glutathione transferases--structure and catalytic activity.

CRC critical reviews in biochemistry·1988
Same journal

Structure-stability relationship in proteins: fundamental tasks and strategy for the development of stabilized enzyme catalysts for biotechnology.

CRC critical reviews in biochemistry·1988
See all related articles

This review details erythrocyte spectrin structure, synthesis, and interactions. It also compares nonerythroid spectrin forms, like brain spectrin, to red blood cell spectrin.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The erythrocyte spectrin membrane skeleton is crucial for red blood cell (RBC) structure and function.
  • Spectrin, a key component, interacts with various proteins to maintain membrane integrity.
  • Nonerythroid spectrins, found in other cell types, share structural similarities but have distinct roles.

Purpose of the Study:

  • To provide a comprehensive overview of erythrocyte spectrin.
  • To explore the structure, synthesis, assembly, turnover, and binding interactions of RBC spectrin.
  • To compare RBC spectrin with characterized nonerythroid spectrins, focusing on chicken intestinal and brain forms.

Main Methods:

  • Literature review and synthesis of existing research.

Related Experiment Videos

  • Comparative analysis of spectrin molecules from different cell types.
  • Examination of spectrin-binding protein interactions.
  • Main Results:

    • Detailed characterization of RBC spectrin structure, synthesis, and interactions with ankyrin, protein 4.1, and actin.
    • Identification and comparison of nonerythroid spectrins, including chicken TW260/240 and brain fodrin.
    • Evidence for two brain spectrin isoforms with distinct locations, structures, and binding partners.

    Conclusions:

    • Spectrin proteins are highly conserved yet functionally diverse across different cell types.
    • Brain spectrin isoforms likely play significant roles in neuronal development, axonal transport, and synaptic transmission.
    • Further research into nonerythroid spectrin functions can elucidate broader cellular mechanisms.