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

Protein-mediated protein maturation in eukaryotes

I G Haas1

  • 1Institut für Biochemie, Heidelberg, Germany.

FEBS Letters
|August 1, 1995
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

Mannosidase action, independent of glucose trimming, is essential for proteasome-mediated degradation of unassembled glycosylated Ig light chains.

Biological chemistry·2001
Same author

Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.

Proceedings of the National Academy of Sciences of the United States of America·2000
Same author

Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity.

Molecular biology of the cell·2000
Same author

Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog.

Biological chemistry·1999
Same author

Cycloheximide, a new tool to dissect specific steps in ER-associated degradation of different substrates.

Biological chemistry·1999
Same author

The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP.

Proceedings of the National Academy of Sciences of the United States of America·1998

Eukaryotic cells utilize heat shock proteins (HSPs), or molecular chaperones, to guide protein maturation from synthesis to final structure and localization. This review discusses cytosolic protein-mediated maturation processes essential for cellular function.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Eukaryotic cells require intricate mechanisms for protein maturation.
  • Protein maturation involves folding, compartmentalization, and structural attainment.
  • Nascent polypeptide chains begin their journey in the cytosol.

Purpose of the Study:

  • To review the strategies employed by eukaryotic cells for protein maturation.
  • To highlight the role of molecular chaperones in protein processing.
  • To discuss protein-mediated processes occurring within the cytosol.

Main Methods:

  • Literature review of protein maturation pathways.
  • Focus on heat shock proteins (HSPs) and molecular chaperones.
  • Discussion of cytosolic protein-mediated events.

Related Experiment Videos

Main Results:

  • Heat shock proteins (HSPs) are key players in protein maturation.
  • These chaperones are constitutively expressed and highly conserved.
  • Cellular strategies ensure proper protein structure and localization.

Conclusions:

  • Molecular chaperones are essential for eukaryotic protein maturation.
  • Cytosolic processes are critical for protein folding and transport.
  • HSPs facilitate the attainment of mature protein structures and cellular destinations.