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Rab Proteins01:14

Rab Proteins

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.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Rab Cascades01:25

Rab Cascades

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.
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
The Ras Gene02:38

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a superfamily...
Mutations01:39

Mutations

Overview
Mutations in Microorganisms01:18

Mutations in Microorganisms

Mutations are heritable changes in an organism’s genome involving alterations in the base sequence of DNA or RNA. These changes can influence cellular processes and phenotypic traits, potentially transforming the unaltered wild type into a mutant form. Such changes, termed forward mutations, are pivotal in shaping the genetic diversity of organisms.RNA viruses exhibit the highest mutation rates due to the absence of robust proofreading mechanisms during genome replication. In contrast,...

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Related Experiment Video

Updated: Jun 23, 2026

Targeted Next-generation Sequencing and Bioinformatics Pipeline to Evaluate Genetic Determinants of Constitutional Disease
09:34

Targeted Next-generation Sequencing and Bioinformatics Pipeline to Evaluate Genetic Determinants of Constitutional Disease

Published on: April 4, 2018

The functional effect of pathogenic mutations in Rab escort protein 1.

Y V Sergeev1, N Smaoui, R Sui

  • 1Ophthalmic Genetics and Visual Function Branch, National Eye Institute, National Institutes of Health, Bethesda, MD, United States.

Mutation Research
|May 12, 2009
PubMed
Summary
This summary is machine-generated.

Choroideremia (CHM) is an X-linked condition causing blindness due to CHM gene mutations. This study identifies new mutations and analyzes their structural impact on REP-1 protein function.

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Last Updated: Jun 23, 2026

Targeted Next-generation Sequencing and Bioinformatics Pipeline to Evaluate Genetic Determinants of Constitutional Disease
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08:55

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

Published on: December 14, 2017

Area of Science:

  • Ophthalmology
  • Genetics
  • Molecular Biology

Background:

  • Choroideremia (CHM) is an X-linked chorioretinal degeneration leading to blindness in affected males.
  • The CHM gene encodes Rab escort protein 1 (REP-1), crucial for cellular protein trafficking.
  • Most known CHM mutations result in a complete loss of REP-1 function.

Purpose of the Study:

  • To identify and characterize novel pathogenic mutations in the CHM gene.
  • To analyze the structural and functional consequences of these mutations on REP-1 protein.
  • To correlate mutation type with phenotypic effects in Choroideremia patients.

Main Methods:

  • Identification of novel CHM gene mutations (missense, truncation, deletions).
  • In silico modeling of human REP-1 3D structure and protein interactions.
  • Western Blot analysis to confirm protein loss in patient cells.

Main Results:

  • Reported four pathogenic CHM mutations: L550P missense, c.1542T>A STOP, c.525_526delAG, and c.1646delC deletions.
  • In silico analysis predicted L550P destabilizes REP-1 structure; truncation/deletion mutants impair function and interactions.
  • Western Blot confirmed reduced REP-1 protein levels in patient mononuclear cells and fibroblasts.

Conclusions:

  • Novel CHM mutations identified, expanding the spectrum of REP-1 dysfunction.
  • Structural modeling provides insights into mutation-induced REP-1 protein instability and loss of function.
  • These findings enhance understanding of Choroideremia pathogenesis and genotype-phenotype correlations.