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Related Concept Videos

Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Protein Complexes with Interchangeable Parts01:57

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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.
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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
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Covalently Linked Protein Regulators02:04

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Covalently Linked Protein Regulators02:04

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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.
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Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
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Multivalency in Rab effector interactions.

Amrita Rai1, Roger S Goody1, Matthias P Müller1

  • 1a Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.

Small Gtpases
|January 28, 2017
PubMed
Summary
This summary is machine-generated.

Rab proteins control cell transport by interacting with effector molecules. Some effectors bind multiple Rab proteins, influencing various cellular processes.

Keywords:
EHBPsGcc185MicalsMyoVRab effectorsRabenosyn-5bMERBmultivalency

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Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Rab proteins are key regulators of vesicular transport in eukaryotic cells.
  • They interact with effector molecules to connect transport to cellular structures and processes.

Purpose of the Study:

  • To provide an overview of Rab effector molecules.
  • To discuss the functions of multivalent Rab:effector interactions.

Main Methods:

  • Literature review of Rab proteins and their effectors.
  • Analysis of existing data on Rab:effector binding.

Main Results:

  • Effectors can bind to multiple Rab proteins simultaneously (multivalent interactions).
  • These interactions are proposed to link Rab proteins to diverse cellular functions.

Conclusions:

  • Multivalent Rab:effector interactions represent an important regulatory mechanism in cellular transport.
  • Further research is needed to fully elucidate the functions of these interactions.