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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,...
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...
Protein Networks02:26

Protein Networks

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mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
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Protein-protein Interfaces

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Related Experiment Video

Updated: May 10, 2026

A High-content Imaging Workflow to Study Grb2 Signaling Complexes by Expression Cloning
10:52

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Published on: October 30, 2012

A Novel Phosphopeptide Microarray Based Interactome Map in Breast Cancer Cells Reveals Phosphoprotein-GRB2 Cell

Srinivasan Krishnamoorthy1, Zhonghua Liu, Ailing Hong

  • 1Department of Biology and Biochemistry, University of Houston, Houston, Texas, United States of America.

Plos One
|July 5, 2013
PubMed
Summary

This study maps protein interaction networks in breast cancer cells, revealing novel signaling pathways and identifying global downregulation of phosphoprotein interactions in metastatic cells, offering potential biomarker and therapeutic targets.

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Area of Science:

  • Cellular biology
  • Molecular signaling
  • Biochemistry

Background:

  • Cellular signaling pathways are complex networks regulated by post-translational modifications like phosphorylation.
  • Understanding phosphoprotein interactions is crucial for deciphering disease phenotypes and physiological hemostasis.
  • A comprehensive map of phospho-motif interactions can identify disease-specific signatures.

Purpose of the Study:

  • To map endogenous tyrosine-phosphoproteome interaction networks in breast cancer cells.
  • To identify novel protein-protein interactions in signaling cascades mediated by GRB2.
  • To investigate the role of phosphoprotein interactions in metastatic potential.

Main Methods:

  • Utilized a novel phosphopeptide microarray technology.
  • Mapped tyrosine-phosphoproteome interaction networks in breast cancer cells.
  • Focused on signaling adaptor protein GRB2 and the Ras-ERK signaling cascade.

Main Results:

  • Identified previously reported and novel motif-specific protein interactions.
  • Observed differential regulation of phospho-motifs across various cell types.
  • Found global downregulation of phosphoprotein interactions in cells with metastatic potential.

Conclusions:

  • Revealed novel phosphoprotein-mediated signaling networks.
  • Highlighted the potential of identified nodes as biomarkers or therapeutic targets.
  • Emphasized the need for further analysis of protein-protein interaction nodes.