part 6 Flashcards
what is the endomembrane system
ER, Golgi, transport vesicles, endosomes, lysosomes.
what are the functions of the endomembrane system
transportation, storage, degradation, and production
what are clathrin
a set of proteins that allow for the formation of the endosome as a pathogen is being taken in.
Found on the surface of the cell.
what is cathepsin
Cysteine proteases
S, L, B, D
Need an acidic environment to be activated (acidification).
what are the four types of cathepsin
S: almost all APCs express this enzyme
L: expressed in thymic cortisol cells (T cell training in thymus)
B and D: plays a role, but not much.
what pathogens bind to MHC I
cytosolic
what pathogens are are presented to CD8 cells
cytosolic
cell death
what pathogens are presented on MHC II
intravesicular and extracellular
what pathogens are presented to CD4 cells
intravesicular and extracellular
how are intravesicular pathogens neutralized
activates killing; endocytic vesicles (low pH)
how are extracellular pathogens neautralized
presenting cell activates B cells to secrete Ig; endocytic vesicles (low pH)
what are TAPs
transports peptides from the cytosol into the endoplasmic reticulum, thereby selecting peptides matching in length and sequence to respective MHC class I molecules
how many TAPs are there
1 and 2
how long are the peptides TAP transports
8-16 AAs long
what are the physical properties of TAP
TAP 1 and 2 transversing the membrane, with ATP binding cassesttes exposed on cytosol side
what is the proteasome complex
Tube-like complex
Degradation complex
Takes chains of amino acids and chops them.
Main type of proteasome completely degrades proteins.
what are the parts of the proteasome complex
The catalytic chamber (20S Core) is where digestion takes place.
Made up of 7 columns; 4 proteins per column.
Ubiquitin protein: highly-conserved, about 73 amino acids long
Targets proteins for degradation (tagging).
19S regulatory particle of proteasome binds to ubiquitin
what is ubiquitin? why is it important
a protein found in most tissues (ubiquitous)
Proteins are marked for degradation by the attachment of ubiquitin to the amino group of the side chain of a lysine residue
what is the immunoproteasome complex for
antigen presenting
what does interferon secretion upregulate
upregulates the amount of MHC I presented on the surface, which allows for upregulation of TAP LMP2 and LMP7, (MECL-1) (core protein)
PA28 (regulatory proteins)
what is the first step of MHC I expression
Partially folded MHC class I alpha chains bind to calnexin (chaperone protein) until B2-microglobulin binds.
what is the second step of MHC I expression
MHC class I alpha:beta complex is released from calnexin, binds to chaperone complexes (calreticulin and ERp57) and binds to TAP via tapasin
what does tapasin do
associates with TAP
what is ERp57
thioreductase (breaking disulfide bonds)