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Rab Cascades

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.

Rab Proteins

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...

Mechanism of Filopodia Formation

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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Phosphoinositides and PIPs

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Fimbriae, Pili, and Axial Filaments

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Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...

Pinching-off of Coated Vesicles

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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

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Related Experiment Video

Updated: Jun 20, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

The dynamic Rab11-FIPs.

Conor P Horgan¹, Mary W McCaffrey

¹Molecular Cell Biology Laboratory, Department of Biochemistry, Biosciences Institute, University College Cork, Cork, Ireland.

Biochemical Society Transactions

|September 17, 2009

Summary

Rab11-family interacting proteins (FIPs) are crucial effectors for Rab and Arf GTPases. This review details their structure, function, and regulation of membrane trafficking.

Area of Science:

Molecular Biology
Cell Biology
Protein Interactions

Background:

Rab11-family interacting proteins (FIPs) are conserved effectors for Rab and Arf GTPases.
FIPs bind Rab11 subfamily members via a Rab11-binding domain (RBD).
Crystal structure reveals FIP homodimerization and heterotetrameric complex formation with Rab11.

Purpose of the Study:

To review the Rab11-FIP field.
To discuss FIP function at molecular and cellular levels.
To summarize recent findings on FIPs' roles in membrane trafficking.

Main Methods:

Literature review of Rab11-FIP research.
Analysis of protein structure and function.
Summary of molecular and cellular studies on FIPs.

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Last Updated: Jun 20, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

In Vitro Polymerization of F-actin on Early Endosomes

In Vitro Polymerization of F-actin on Early Endosomes

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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

Main Results:

FIPs form heterotetrameric complexes with Rab11 via homodimerization.
FIPs are categorized into Class I (Rip11, FIP2, RCP) and Class II (FIP3, FIP4).
FIPs regulate diverse membrane trafficking events.

Conclusions:

FIPs are key regulators of membrane trafficking.
Understanding FIP structure and function is critical for cell biology.
Further research will elucidate FIPs' precise roles in cellular processes.