Block 1 Lecture 6 Flashcards
how many hydrophobic transmembrane spans does a G protein coupled receptor have
7
how many hydrophobic transmembrane spans does a CTFR have
12
what is the function of the Golgi and rough ER
making and moving proteins
what happens to proteins in the golgi
the enter at the cis face, the Golgi modifies sorts and packages raw proteins, they exit the trans face
what is a trimer ion channel
epithelial Na+ channel
what is a tetramer ion channel
voltage gated Na+, K+, Ca2+ channels
what is a pentameter ion channel
nicotinic Ach receptor
what is a hexameter ion channel
hemi junction or connexon
what happens in O linked glycosylation
adding sugar units on serine
what happens in N linked glycosylation
adding ogliosaccharide to an asparagine
what happens in GPI linkage
an enzyme cuts and attaches to an asparagine
what is a glycocalyx
formed from proteoglycans on endothelial cells on lining of blood vessels
what does a glycocalyx do
protects and detects strain to cytoskeleton
what happens in cotranslation targeting of secretory proteins to the ER
- signal sequence emerges from the ribosome, recognized and bound by SRP
- the SRP escorts the complex to the ER membrane where it binds to SRP receptor
- the SRP is released, the ribosome binds to a membrane translocation complex of sec61 proteins and the signal sequence is inserted into a membrane channel
- translation resumes and the growing polypeptide chain is translocated across the membrane
- cleavage of the signal sequence by signal peptidase releases the polypeptide into the lumen of the ER
how are proteins deposited straight from the ribosome into the ER
translocon mechanism