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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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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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The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
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The human heart, despite its modest size and weight, is an organ of remarkable strength and endurance. Roughly the size of a fist, the heart weighs between 250 and 350 grams and is nestled within the mediastinum, the medial cavity of the thorax. It extends obliquely for about 12 to 14 cm, resting on the superior surface of the diaphragm. The heart is positioned anterior to the vertebral column and posterior to the sternum, with two-thirds of its mass lying to the left of the midsternal line.
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Rab 10-a traffic controller in multiple cellular pathways and locations.

Christelle En Lin Chua1, Bor L Tang2,3

  • 1Singapore Nuclear Research and Safety Initiative, National University of Singapore, Singapore.

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Summary
This summary is machine-generated.

Rab10, a unique Rab GTPase, defies typical membrane traffic roles by participating in diverse cellular processes. This review explores Rab10

Keywords:
GLUT4Rab10ciliaendoplasmic reticulumneurite outgrowthpolarized transport

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Rab GTPases regulate eukaryotic membrane traffic, typically with restricted functions and localizations.
  • A clear distinction usually exists between exocytic and endocytic Rab proteins.

Purpose of the Study:

  • To review the diverse functions and subcellular localizations of the Rab protein, Rab10.
  • To discuss the molecular mechanisms underlying Rab10's multifaceted roles in cellular transport.

Main Methods:

  • Literature review of studies on Rab10 function and localization.
  • Synthesis of findings from various cell types and biological processes.

Main Results:

  • Rab10 exhibits anomalous behavior, participating in both exocytic and endocytic pathways.
  • Involved in polarized exocytosis, Glut4 transport, axonal growth, and phagocytosis.
  • Localizes to ER, Golgi/TGN, endosomes, phagosomes, and primary cilia.

Conclusions:

  • Rab10 plays a crucial, versatile role in cellular membrane transport.
  • Understanding Rab10's diverse functions is key to deciphering complex cellular processes.