COPII

COPII is a type of vesicle that transports proteins from the rough endoplasmic reticulum to the Golgi apparatus. The name "COPII" refers to the specific coat protein complex that initiates the budding process. The coat consists of large protein subcomplexes that are made of four different protein subunits.

Coat Proteins
There are two protein heterodimers that form the coat complex. These proteins are It should be noted that these proteins alone are not able to cause the budding of the vesicle or direct the vesicle to the correct target membrane. Other proteins are needed for these processes.
 * Sec23p/Sec24p Heterodimer
 * Sec13p/Sec31p Heterotetramer

Budding Process
The GTPase Sar1p is a protein that hydrolyzes GTP and acts like a molecular "switch" that flips between an activated and membrane embedded GTP-bound form, and inactive and soluble GDP-bound form. Inactive GDP-bound Sar1p is attracted to the cytosolic side of the endoplasmic reticulum (ER) membrane by Sec12p. Sec12p is a guanine nucleotide exchange factor, or GEF, and a transmembrane protein residing in the ER membrane. This binding event causes Sar1p to release GDP, and since the concentration of GTP is much higher than GDP in the cytosol, GTP spontaneously binds to Sar1p. Now in a GTP bound state, Sar1p undergoes a conformational change which exposes a hydrophobic tail that can be inserted into the lipid bilayer, binding it to the membrane. Once Sar1p is bound to the membrane the coat protein complexes Sec23p/24p and Sec13p/31p bind to the membrane sequentially. These proteins simultaneously contact Sar1p and cargo proteins destined for the cis-golgi membrane. The Sec23p/24p-Sec13p/31p-Sar1p complexes then coalesce to form a much larger complex. This network deforms the membrane enough to bud a vesicle off.

At some currently unknown point the GTPase Sar1p hydrolyzes it's bound GTP into GDP. This process is required before the vesicle can bud off from the membrane.