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Short-distance Transport of Resources02:12

Short-distance Transport of Resources

Short-distance transport refers to transport that occurs over a distance of just 2-3 cells, crossing the plasma membrane in the process. Small uncharged molecules, such as oxygen, carbon dioxide, and water, can diffuse across the plasma membrane on their own. In contrast, ions and larger molecules require the assistance of transport proteins due to their charge or size. Transport across membranes also occurs within individual cells, playing a variety of essential roles for the plant as a whole.
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Related Experiment Video

Updated: Jul 12, 2026

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation (BiFC) System
08:21

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Published on: September 16, 2011

Evidence for direct interaction between Sprouty and Cbl.

E S Wong1, J Lim, B C Low

  • 1Signal Transduction Laboratory, Institute of Molecular and Cell Biology, National University of Singapore, Singapore 117609, Singapore.

The Journal of Biological Chemistry
|October 29, 2000
PubMed
Summary
This summary is machine-generated.

Human SPRY2 protein interacts with c-Cbl, a key regulator of receptor tyrosine kinase signaling. This interaction modulates epidermal growth factor receptor internalization, suggesting a role for Sprouty proteins in cellular signaling pathways.

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Last Updated: Jul 12, 2026

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Interactions

Background:

  • Sprouty (SPRY) proteins are known antagonists of receptor tyrosine kinase (RTK)/Ras/MAPK pathways.
  • Four mammalian Sprouty genes exist, sharing conserved domains with Drosophila homologs.
  • The precise mechanism of Sprouty-mediated signaling regulation remains incompletely understood.

Purpose of the Study:

  • To identify proteins interacting with human SPRY2 (hSPRY2).
  • To elucidate the mechanism of Sprouty protein down-regulatory effects.
  • To investigate the functional consequences of hSPRY2-protein interactions.

Main Methods:

  • Protein-protein interaction assays to identify binding partners of hSPRY2.
  • Mapping of binding domains between hSPRY2 and identified interacting proteins.
  • Functional assays measuring receptor tyrosine kinase (RTK) signaling, specifically epidermal growth factor receptor (EGFR) internalization.

Main Results:

  • hSPRY2 directly associates with c-Cbl, a known RTK signaling down-regulator.
  • A specific N-terminal sequence of hSPRY2 binds to the Ring finger domain of c-Cbl.
  • hSPRY2 binding to c-Cbl abrogated c-Cbl-induced EGFR internalization; a non-binding mutant hSPRY2 showed no effect.

Conclusions:

  • hSPRY2 directly interacts with c-Cbl, suggesting a novel mechanism for RTK pathway regulation.
  • The interaction between hSPRY2 and c-Cbl modulates EGFR internalization, a key process in receptor-mediated endocytosis.
  • Sprouty proteins may function by modulating the activity of key signaling regulators like c-Cbl.