Related Experiment Video
Updated: Jun 6, 2026
17:14
In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
Intersectin multidomain adaptor proteins: regulation of functional diversity
Liudmyla Tsyba1, Oleksii Nikolaienko, Oleksandr Dergai
1Department of Functional Genomics, Institute of Molecular Biology and Genetics, NASU, 150 Zabolotnogo Street, Kyiv, Ukraine.
Gene
|December 15, 2010
Summary
Intersectins (ITSNs) are adaptor proteins crucial for cell signaling and vesicle transport. This review highlights their diverse roles in neuronal and non-neuronal cells, emphasizing their importance in cellular processes and disease.
Area of Science:
- Cell Biology
- Molecular Biology
- Neuroscience
Background:
- Adaptor/scaffold proteins assemble multiprotein complexes, regulating signaling cascades.
- Intersectins (ITSNs) are conserved adaptor proteins involved in endo/exocytosis, actin rearrangement, and signal transduction.
Purpose of the Study:
- To review recent advances in the function of ITSNs.
- To explore the structural and functional diversity of ITSNs.
- To discuss the relevance of ITSNs in neurodegenerative diseases and cancer.
Main Methods:
- Literature review of recent advances in ITSN research.
- Analysis of alternative splicing and transcription in ITSN regulation.
- Examination of ITSN expression patterns and protein interactions.
Main Results:
- ITSNs play significant roles in both neuronal and non-neuronal cells.
- Alternative splicing and transcription generate diverse ITSN isoforms.
- ITSNs interact with various proteins, influencing vesicle trafficking and signaling.
Conclusions:
- The regulation of ITSN expression and specificity is diverse across cell types.
- ITSN proteins are critical for vesicle trafficking and signal transduction.
- Dysregulation of ITSNs may be relevant to neurodegenerative diseases and cancer.
Related Concept Videos
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:30Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
02:26Conservation of Protein Domains Over Different Proteins
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.