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 Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.2K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.2K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.4K
14.4K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

311
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
311
Protein Complex Assembly02:41

Protein Complex Assembly

16.0K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.0K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.1K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.1K
Amyloid Fibrils03:03

Amyloid Fibrils

11.4K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
11.4K

You might also read

Related Articles

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

Sort by
Same author

CacyBP/SIP - RPL6 interaction: potential influence on ribosome function.

Amino acids·2025
Same author

Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

S100 Proteins-Intracellular and Extracellular Function in Norm and Pathology.

Biomolecules·2024
Same author

Conformational changes in the Niemann-Pick type C1 protein NCR1 drive sterol translocation.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Involvement of CacyBP/SIP in differentiation and the immune response of HaCaT keratinocytes.

Immunobiology·2023
Same author

S100A6 Protein-Expression and Function in Norm and Pathology.

International journal of molecular sciences·2023

Related Experiment Video

Updated: Dec 6, 2025

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

3.1K

HSP90 Co-Chaperone, CacyBP/SIP, Protects α-Synuclein from Aggregation.

Anastasiia Bohush1, Anna Filipek1

  • 1Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Street, 02-093 Warsaw, Poland.

Cells
|October 14, 2020
PubMed
Summary

CacyBP/SIP protein protects alpha-synuclein from aggregation, a key factor in Parkinson's disease. This protein may play a significant role in treating synucleinopathies.

Keywords:
CacyBP/SIPParkinson’s diseaseprotein aggregationα-synuclein

More Related Videos

Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

17.6K
Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models
08:44

Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models

Published on: November 11, 2014

8.4K

Related Experiment Videos

Last Updated: Dec 6, 2025

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

3.1K
Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

17.6K
Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models
08:44

Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models

Published on: November 11, 2014

8.4K

Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • CacyBP/SIP protein functions as an HSP90 co-chaperone with intrinsic chaperone properties.
  • CacyBP/SIP has demonstrated protective effects against protein aggregation and denaturation in vitro.
  • Alpha-synuclein aggregation in Lewy bodies is a hallmark of Parkinson's disease.

Purpose of the Study:

  • To investigate the influence of CacyBP/SIP on alpha-synuclein aggregation.
  • To determine the role of CacyBP/SIP in cellular models of Parkinson's disease pathology.
  • To explore the direct interaction between CacyBP/SIP and alpha-synuclein.

Main Methods:

  • Thioflavin T (ThT) fluorescence assay to monitor alpha-synuclein aggregation.
  • High-speed ultracentrifugation, dot-blot, and transmission electron microscopy (TEM) for structural analysis.
  • Proximity ligation assay (PLA) and in vitro assays with purified proteins to assess interactions.

Main Results:

  • CacyBP/SIP significantly inhibits alpha-synuclein aggregation, particularly in the initial phase.
  • A specific fragment of CacyBP/SIP (N-terminal and CS domain) is crucial for its protective activity.
  • Overexpression of CacyBP/SIP in HEK293 cells reduced alpha-synuclein inclusions and enhanced cell viability against rotenone.
  • Direct interaction between CacyBP/SIP and alpha-synuclein was confirmed both in vitro and in cellulo.

Conclusions:

  • CacyBP/SIP directly interacts with alpha-synuclein and protects it from aggregation.
  • The N-terminal and CS domain of CacyBP/SIP are essential for its anti-aggregation function.
  • CacyBP/SIP demonstrates potential therapeutic relevance for Parkinson's disease and other synucleinopathies.