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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein 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...
Protein Complexes with Interchangeable Parts01:57

Protein 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...
Mismatch Repair01:36

Mismatch Repair

Overview
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
Mismatch Repair01:36

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Covalently Linked Protein Regulators02:04

Covalently 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.

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Sprouty proteins: modified modulators, matchmakers or missing links?

G R Guy1, R A Jackson, P Yusoff

  • 1Signal Transduction Laboratory, Institute of Molecular and Cell Biology, Proteos, Room 3-14B, Singapore, Republic of Singapore 138673.

The Journal of Endocrinology
|May 9, 2009
PubMed
Summary
This summary is machine-generated.

Sprouty proteins regulate organ development by inhibiting the Ras/Erk pathway. Their function is controlled through covalent modifications, including ubiquitination, influencing their location, stability, and interactions.

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Area of Science:

  • Cellular signaling
  • Developmental biology
  • Protein regulation

Background:

  • Sprouty proteins are key regulators of organogenesis, particularly endothelial tube branching.
  • They act downstream of receptor signaling to inhibit the Ras/Erk pathway.
  • The precise mechanisms of Sprouty protein function and their interactions remain incompletely understood.

Purpose of the Study:

  • To elucidate the functional mechanisms of Sprouty proteins.
  • To identify key protein interactions and regulatory pathways involving Sprouty.
  • To understand how Sprouty proteins are regulated through post-translational modifications.

Main Methods:

  • Analysis of conserved domains within Sprouty proteins (TKB binding motif, SRM, CRD).
  • Identification of interacting partners, including kinases, phosphatases, and ubiquitin ligases.
  • Investigation of Sprouty protein covalent modifications, such as phosphorylation and ubiquitination.

Main Results:

  • Sprouty proteins possess distinct domains (TKB, SRM, CRD) mediating interactions with various proteins.
  • Serine/threonine kinases bind to the SRM, while protein phosphatase 2A interacts with the TKB motif.
  • Ubiquitin E3 ligases (c-Cbl, SIAH2) bind to the N-terminus, targeting Sprouty for ubiquitination and degradation.

Conclusions:

  • Sprouty protein function is tightly regulated by extensive covalent modifications.
  • These modifications control Sprouty protein localization, stability, and interactions.
  • Sprouty proteins act as facilitators, bringing together key signaling components for precise regulation.