PROTEIN TARGETTING

Septelia Inawati Wanandi

Proteins are translated and modified with in the rough endoplasmic

reticulum. In order to complete their modifications, they are transported
in membrane-bounded vesicles to the cis side of the Golgi apparatus

Transport vesicles from the rough ER fuse together and become

the cis cisterna of the Golgi.

Once they reach the Golgi apparatus, additional modifications are made to
the transported proteins by resident Golgi enzymes. These modifications
are key in ensuring the proteins reach their final destinations once they
leave the Golgi apparatus.

The Golgi apparatus is divided into distinct regions. These include

the cis cisterna, nearest the ER, the centrally located medial
cisternae, the trans cisterna, and the trans Golgi Network (TGN).

According to the cis maturation model, the proteins are transported

through the Golgi stack as the cisterna containing them migrate, or
mature, in a cis-to-trans direction. New vesicles from the ER continually
supply new cis cisterna as trans Golgi network vesicles mature.

Within the trans Golgi network, proteins are sorted by their final
destinations. This is accomplished by receptor molecules
embeddedin the membrane of the TGN.

When proteins have reached their correct location within the TGN, the
membrane at those locations buds off into vesicles. More than one
protein can be contained within each transport vesicle.

Once released, the vesicles carry their cargo proteins to a final location.
Possible destinations include the lysosome, the digestive organelle of the
cell, and the plasma membrane, where the proteins can be released
elsewhere in the organism.

Summary
Targeting of newly synthesized proteins is an integral component of protein
synthesis.
In prokaryotes, targeting is usually achieved by an N-terminal signal sequence of
about 20 mostly hydrophobic amino acids.

In eukaryotes, targeting is more complex due to the large number of different

cellular compartments:
- Nuclear targeting via the nuclear pore using a nuclear localization signal.
- ER targeting (secretory pathway) via N-terminal signal sequences using
SRPs with subsequent attachment to the ER,
- Followed by transport to the Golgi complex
Protein degradation of damaged or obsolete proteins is carried out by
lysosomes, vesicles filled with degradating enzymes in a ubiqutin-dependent
process by specific proteases in a large cytosolic complex called the
proteasome.