Ans 2. The secretory pathway refers to the
ER(Endoplasmic reticulum), Golgi
Apparatus, and the vesicles that travel in between them as
well as the cell membrane.
It’s named ‘secretory’ for being the pathway by which the cell
secretes proteins into the extracellular environment.
- This pathway also processes proteins that will be
membrane-bound (whether in the cellular membrane or in the ER or
Golgi membranes themselves), as well as lysosomal enzymes, and also
any proteins that will live their lives in the secretory pathway
itself.
- It is responsible for the processing of proteins for export
from the cell.
- The synthesis of all proteins begins in the cytosol
compartment.
- For proteins entering the secretory pathway, the first step is
targeting to the endoplasmic reticulum.
Co-translational translocation.
- Synthesis of proteins entering the endoplasmic reticulum is
initiated on free ribosomes.
- A targeting sequence of hydrophobic amino acids near the
amino-terminal end of the growing polypeptide results in the
binding of the ribosome to the ER membrane and in the insertion of
the polypeptide into the endoplasmic reticulum.
- Targeting to the endoplasmic reticulum begins
with a special sequence at the very N-terminus, the beginning of
the protein, which tends to be somewhat apolar or hydrophobic this
signal peptide sequence (a sequence of at least
eight hydrophobic amino acids at the amino-terminal end of the
polypeptide) draws a Signal recognition particle(SRP) while the
protein is still being synthesized on the ribosome.
- This greatly reduces the rate of translocation and allows the
ribosome to attach to the endoplasm reticulum by means of a special
SRP receptor in the ER membrane.
- The ribosome becomes attached to a ribosome receptor that also
functions as a translocation channel for the newly synthesized
polypeptide
- The synthesis pauses while the ribosome-protein complex is
transferred to an SRP receptor on the ER.
- As the ribosome becomes attached, the SRP is removed and
translation resumes.
- The nascent protein is then inserted into the translocon, a
membrane-bound protein conducting channel composed of the Sec61
translocation complex.
- In secretory proteins and type, I transmembrane protein the
signal sequence is immediately cleaved from the nascent polypeptide
once it has been translocated into the membrane of the ER.
- The signal sequence of type II membrane proteins and some
polytopic membrane proteins are not cleaved off and therefore are
referred to as signal anchor sequences.
- Within the ER, the protein is first covered by a chaperone
protein to protect it from the high concentration of other proteins
in the ER, giving it time to fold correctly inside the lumen of the
ER.
- Once folded the protein is modified as needed then transported
to the Golgi for further processing and goes to its target
organelles or is retained in the ER by various ER retention
mechanisms.
Post-translational translocation
- Most secretory proteins use the above pathway to enter the ER,
but some proteins are translated into the cytosol and then later
transported to ER.
This way the proteins are targetted to the secretory
pathway.