Unit 04 Pt2
Introduction
Overview of Unit 4, part 2 in BIO 331.
Previous discussions focused on protein coats on vesicles used for cellular trafficking and transport.
Importance of Membrane Curvature
Membrane bending and curvature are critical for vesicle formation (vesiculation).
Additional proteins called BAR domains play an essential role in membrane curvature.
BAR Domain Functions
BAR domains can form dimers that assist in curvature formation during vesiculation.
They contain alpha helices that wedge into the cytoplasmic leaflet to induce membrane curvature.
Vesicle Pinching Off
Vesicles must pinch off from donor membranes.
This process is facilitated by dynamin proteins.
Dynamin Structure and Function
Dynamin proteins have two key domains:
PIP binding domain
GTPase domain
They utilize GTP hydrolysis as energy to facilitate membrane pinching, leading to the fusion of non-cytosolic leaflets.
Historical Context
Early research by David Suzuki on Drosophila mutants revealed insights into endocytosis.
Mutant forms of dynamin hindered vesicle recycling and neurotransmitter release, causing paralysis.
Electron micrographs showed accumulation of vesicles at the membrane due to ineffective pinching off.
Uncoating of Vesicles
After pinching off, vesicles shed their coats, typically clathrin, in a rapid manner.
This process is aided by the PIP phosphatase co-packaged within vesicles, which weakens the association between adapter proteins and facilitates uncoating.
Hsp70 proteins may also function as ATPase for uncoating.
Stability of Coats
Different vesicle coats exhibit varying stability, with clathrin-coated vesicles being particularly notable for their stability during formation.
Role of PIP and Regulatory Mechanisms
PIP production is crucial for regulating clathrin assembly and coat formation alongside adapter proteins.
Other regulatory contexts include coat recruitment GTPases that manage coat assembly on endosomes and Golgi membranes.
GTPase Functionality
GDP-binding proteins act as molecular switches:
GTP-bound form is active.
GDP-bound form is inactive.
GTPase-activating proteins (GAPs) facilitate the deactivation of GTP into GDP.
Monomeric GTPases and Vesicle Formation
Monomeric GTPases such as SAR1 play a crucial role in vesicular transport and have distinct activating proteins for COPI and COPII vesicles.
The transition between GDP and GTP states is essential for their function.
SAR1 Activation Process
SAR1 transitions from an inactive GDP-bound state to an active GTP-bound state, leading to a conformational change that allows insertion into the membrane.
Active SAR1 recruits additional proteins (Sec23 and Sec24) that further aid in coat assembly and vesicle formation.
COPII Coat Assembly
COPII coat assembly involves additional proteins (Sec13 and Sec31) forming an outer shell, analogous to clathrin structures.
The transition between active and inactive states (GTP to GDP) is regulated through GTPase activity.
Assembly vs. Disassembly
The assembly of vesicle coats must outrun disassembly to ensure efficient trafficking of vesicles.
COPII coats are generally more stable compared to clathrin and COPI coats, with slower shedding post-pinching.
Tubular Vesicle Formation
Vesicular structures can vary in shape, with examples like tubular vesicles forming around linear proteins such as collagen.
Live cell imaging studies exhibit the formation of these tubular structures from the trans Golgi network.
RAB Proteins and SNAREs
RAB proteins act as markers for specific vesicular transport and are key players in identifying destination compartments.
SNARE proteins mediate the membrane fusion process at target sites.
RAB Protein Functionality
RAB proteins have distinct roles in facilitating docking and fusion of vesicles, utilizing GEFs for activation.
RAB proteins stay bound to GDP when inactive and are tethered by GDI for solubility.
Interactions and Complexity of RAB Proteins
The interplay of RAB proteins with effectors and SNAREs highlights the complexity of vesicular transport.
Specific examples show RAB proteins binding to multiple effector proteins, showcasing functional diversity.
Conclusion
Summary of vesicular transport mechanisms and the specificity involved in trafficking to various cellular compartments.