Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular

Related Experiment Video

Updated: May 1, 2026

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
10:26

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

10.6K

E Peles1, J Schlessinger, M Grumet

  • 1Dept of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel. peles@wiccmail.weizmann.ac.il

Trends in Biochemical Sciences
|May 19, 1998
PubMed

Insights

Receptor-like protein tyrosine phosphatase beta (RPTP beta) interacts with cell adhesion molecules and extracellular matrix proteins. These interactions are key for cell recognition, intercellular signaling, and regulating RPTP activity through cell contact.

Area of Science:

  • Molecular biology
  • Cell biology
  • Neuroscience

Background:

  • Receptor-like protein tyrosine phosphatase beta (RPTP beta) shares similarities with cell adhesion molecules (CAMs).
  • RPTP beta plays a role in neuronal development and function.
  • Understanding RPTP beta's interactions is crucial for cell communication.

Purpose of the Study:

  • To explore the role of RPTP beta in forming cell-recognition complexes.
  • To discuss the implications of these complexes in intercellular signaling.
  • To examine how cell-cell and cell-extracellular matrix (ECM) contact regulates RPTP beta activity.

Main Methods:

  • Literature review and analysis of existing research on RPTP beta.
  • Comparative analysis of RPTP beta structure and function with CAMs.
  • Discussion of experimental evidence regarding RPTP beta interactions.

Main Results:

  • RPTP beta binds to various neuronal CAMs and ECM proteins.
  • These interactions facilitate the formation of cell-recognition complexes.
  • Cell-cell and cell-ECM contacts are identified as regulators of RPTP beta activity.

Conclusions:

  • RPTP beta is a key component in cell recognition complexes.
  • These complexes are vital for mediating intercellular signaling pathways.
  • RPTP beta activity is dynamically regulated by its cellular environment and adhesion interactions.

More Related Videos

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes09:40

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

13.9K
Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors08:45

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Published on: July 17, 2020

5.7K

Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly 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,...
4.7K
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
4.7K
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
6.1K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
15.3K
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
15.5K
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
4.4K