-
Ran
a small GTPase that regulates cargo binding and release on exprtins and importans, based on whether it is in GTP or GDP from
-
basic unit of DNA packaging
nucleosome
-
composed of intermediate filaments and provides mechanical support for the nuclear membrane
nuclear lamina
-
these 3 sequences are required to produce a eukaryotic chromosome that can be replicated and the seperated during mitosis
telomere, replication origin and centromere
-
targetting signal
unique N terminal AA sequence required for a protein to be directed to a specific organele
-
these recognize targetting signals on proteins, bind them and shuttle them to the nuclear pore complex for export or import
importins and exportins
-
How do ribosomal proteins that were shuttled into the nucleus get back out after ribosomal assembly
during assembly the NLSs are 'hidden' inside the structure of the ribosome
-
phospholipid composition
glycerol backbone, 2 non polar FA hydrocarbon tails and a phosphate containing head group
-
coline containing phospholipids
sphingomyelin and phophotidylcholine
-
molecules made in the smooth er
- -all cholesterol
- -most phospholipids (initally on the cytoplasmic half because enzymes ans substrates are in the cytoplasm)
- -also involved heavily in detox reactions (50% with peroxisomes handling the other 50%)
-
intergral proteins
- -require an alpha helical domain of hydrophobic amino acids(at least 20 to pass all the way thru membrane)
- -can pass through once or multiple times
- CAN ONLY BE ROMOVED WITH THE USE OF A DETERGENT
-
covalently tethered integral membrane proteins
largely exposed and are COVALENTLY tehterd to either a phospholipid or glycolipid
-
glycosylation
- -occurs in the lumen of the er(N) and golgi(N and O)
- -CHO is always found is outer leaflet of the plasma membrane (because enzymes that add the carb are inside the lumen of said organelles)
-
lipid rafts
-compostion
-size
- c-mostly sphingomyelin (choline containing) and cholesterol, also some phosphotidylcholine
- s- thicker than the phospholipid bilayer
-
lipofuscin
bodies present in many undividing cells made up of residual bodies of lysosomal degredation
-
intermediate filaments
function
structure
pathology
- f-mechanical strength
- s- thought to be 8 tetramer filaments woven into a rope like structure
- p- can be used to determine origin of tumor cells because different cell types have different IF
-
IF types and cell types (6)
- Keratins Epithelium
- Vimentin Mesenchymal cells
- Desmin Muscle
- Gilial fibrillary Glial cells
- Neurofilaments Neurons
- Nuclear lamins surrounding internal NM NUCLEAR LAMINS ARE FOUND IN ALL CELLS TYPES
-
centrosome
- microtubule organzing center
- anchors minus end of a microtubule
- has a pair of centrioles perpendicular to eachother
-
kinesin
- MT motor that moves toward the + end of a MT (away from centrosome)
- ATP driven
-
Dynesin
- MT motor that moves toward the - end of a MT (toward centrosome)
- ATP driven
-
microtubule
function
structure
construction
- f-determines postion of organelles and directs transport
- s- 13 profilaments form a hollow MT
- c- gamma tubulin provides nucleus and starts negative end, beta/alpha subunits attach(GTP) and detach(GDP) only at positive end
-
cilia and flagella
structure
construction
function
- -made of MT in a (9+2) arrangement
- -anchored to cell membrane by a basal body (which has same structure as centrioles- 9 sets of triplets)
- f- movement- DYNEIN, using ATP, slides one doublet past another creating bend
-
microfilaments
- determine cell shape
- made of actin, the most abundant protein inside cells
- grows and shrinks at - and + ends
- goverened by ARPs
-
spectrin
actin binding protein that forms supporting network for plasma membrane of RBC
-
Taxol
- defects mitotic spindle
- prevents mitosis by stabalizing MT polymer and preventing dissasembly and thus cell division
- binding site on beta tubulin
-
cytochrome c
- mobile in the intermembrane space of a mtch
- its release will signal apoptosis
-
mitochondrial dna
- 37 genes
- 2 rRNA, 22 tRNA and 13 protein
-
cardiolipin
- combo of 2 phopholipds that are combined in the mtch to strengthen the IMM to withstand the PMF
- -an example of a PL not made in the ER
-
3 special structures of lysosomal membrane
- -H+ pump- to keep acidic inner environmetn required to activate enzymes
- -glycoprotein coat- protects inner membrane from acidic environment
- -transport channels- eject broken down molecules
-
Tay Sachs
results from a absence of hexosaminidase A, which breaks down glycolipids in the lysosome
-
peroxisomes
-ez
-function (3)
-structure
-abundance
-O2 requirement
- -contain catalase
- -beta oxidize FA (as do mtch), syn bile, syn
- PLASMOLAGENS USED IN MYELIN
- -have a single membrane(not present in neurons)
- -can adapt very fast to change in conditions (ie ingestion of EtOH)
- -2nd major O2 user next to mtch
-
checkpoints in cell division
G1/S - (before replication) environment is assessed for favorable conditions, is DNA intact
G2/M- (before division)DNA is checked for completion and accuracy, is DNA intact
-
prometaphase signals what
disappearance of nuclear envelope
-
metaphase plate
when the chromosomes are lined up in the center of the cell
-
cohesins
hold sister chromatids together and are degraded at anaphase allowing SC to be pulled apart
-
condensin
condenses DNA, only active during M phase
-
anaphase A
- - MT shorten to pull SC apart by motor proteins on the kinetocore
- - SC acually roll down MT toward pole with the help of a motor protein that is part of the kinetochore
-
anaphase B
mitotic spindles pulled apart toward the cell wall via motors on the centrosome and on the MT anchoring the centrosome to the periphery
-
when do sister chromatids divide
metaphase/ anaphase transition
-
kinetochore
proteins that attach to the centromere of a chromosome and connect to (+) MT during cell division
-
actin role in mitosis
form contractile ring during cytokinesis
-
what triggers the dissasembly of the nuclear envelope
phosphorylation of lamins
NE disassembly happens at prometaphase
-
this normal cellular process continues during mitosis even when all others have stopped
ATP production in the mitochondria
-
key differences between necrosis and apoptosis (4)
- apoptosis- dying cell phagocytosed
- no inflammation or damage to adjacent cells
- PM stays intact through whole process
- cell shrinks
-
caspases (4)
- -ALWAYS activated during apoptosis
- - cys proteases that degrade the insides of the cell
- -always around inactive, waitng to be activated
- -can cause cascade, activating other caspases
-
BCL2 proteins (2)
- -REGULATE APOPTOSIS in a pro- and anti- manner
- - when deprived can cause OMM to become permeable, thus releasing cyt c, which will activate caspases
-
'eat me' signal
- phosphotidylSERINE on external leaflet of membrane, put there by a non-specific scramblase
- -ALWAYS HAPPENS WITH APOPTOSIS
-
how does mtch get its lipids and proteins
- -via non specific transport proteins (non targetting)
- -NO SNARES on mitochondria so there can be NO VESICULAR transport from ER or golgi
- -mtch channels are only wide enough for UNFOLDED AA to go thorugh
-
Protein folding for organelles
always folded prior to intake into organelle except in the case of mtch
-
how does the nuclear membrane get its lipids
diffusion
-
cyt p450
enzyme in SER involved in detox reactions
-
ER sequesters what
intracellular Ca
-
what forms the cis golgi
ER vesicles
-
ER signalling sequence
required to enter the secratory pathway and is at least 8 hydrophobic aa long
-
SRP
- -recognizes ER signal sequence and shuttles ribosomes that are translating proteins with ER signal sequence to the ER and aid connections and opening translocon channels
- -translation stops while SRP is bound
-
glutathione
prevents disulfide bonding from occuring in the cytosol
-
GPI anchor
added in ER, can act as a sorting signal to direct membrane proteins to specific areas of the PM(lipid raft, calveoli)
-
cotranslational transport
membrane proteins that enter the secratory pathway, mtch membane proteins do not go this route
-
hsp-70 and BIP
- -binding proteins that aid protein folding by binding temporarily to hydrophobic regions
- -hsp-70 in cytosol
- -BIP in lumen of the ER, release is required to exit ER
- -will give up if protein wont properly fold and protein will be ubiquitinated
-
CFTR
transmembrane Cl- channel that is defective in cystic fibrosis. It is not that the channel is non-functional, rather it slightly misfolds and is never released from BIP and is stuck in the ER then degraded
-
what acts as the sorting staion
trans golgi
-
clathrin
-involved in endocytosis from PM and movement from trans golgi to the endosome
-a type of coat protein that will initiate budding, by covering outside and then must fall off to allow fusion
-not part of constitutive p/w
-
SNARES
- -two types V(vesicle) and T(target)
- -complimentary pairs, that excrude water when they bind and allow membranes to fuse
- -targetting signals(and receptors) of vesicles
- - no T-SNARES on mtch or mitochondria
-
Rabs
tethering proteins that aid connection of complimentary SNARE joining
-
sialic acid
- -groups on glycoproteins and glycolipids that give the outer leaftlet its negative charge
- - added in the golgi
-
where are glycolipids formed
formed in the golgi
-
glycocalyx
thick layer of CHO that gives a 'cushion' to the PM
-
M6P funciton and how is it attached and detached
- mannose 6 phosphate- targetting signal for lysosome
- -added to N linked sugar(which is added in the ER) on the acid hydrolase in the cis-golgi.
- -in the trans glogi M6P binds a M6PR, which destines it for the lysosome
- - acid hydrolase is disassociated from the M6PR in the low pH of the lysosome, M6PR is then recycled
-
How are worn out organelles degrades
by the lysosome in autophagosomes
-
GPI-linked proteins cluster here
- lipid rafts
- (glycophphotidylinositol)
-
adaptin
binds cytosolic side of certain receptors as well as clarithrin, thus starting endocytosis
-
LDL receptor
internalization
location
- -internalized by receptor mediated endocytosis
- - localized in the coated pits even before binding it ligand (LDL)
-
ligand and EGF receptor(along with most other signalling receptors) fate after binding
unlike LDLr, the ligand and EGFr(and most other signalling receptors) are targetted to the lysosome for degradation, this is one way to down regulate receptors, by not recycling them
-
caveolae
features
function
location
- - NEVER FUSE WITH LYSOSOMES(think microbe entry, INDISTINGUISHABLE FROM LIPID RAFTS
- -act as signalasomes
- -small invaginations of PM, seen especially in endothelial cells, but absent in neurons
- - maintained by caveolin
-
ribosomes
- made of rRNA(made in nucleolus)
- large subunit- 3 rRNAs and proteins
- small subunit- 1 rRNA and proteins (18s)
-
MT
- -start at gamma tubulin at - end of MT located in the MTOC
- - grow and shrink on + end
- - target of many anti cancer drugs(prevent mitotic spindle formation)
-
actin
- - grow at + end, shrink at - end
- - shape PM
- - form microvilli
- - make lamellipodia
- - contraction causes invagination during division
-
chromosomes with rRNA knobs
13, 14, 15, 21, 22
-
kinetochore
binding site for + ends of MT so sister chromatids can be pulled apart
-
proteins translated in cytosol
- - those destined for the cytosol, peroxisome and mitochondria
- **mtch recieves NO vesicular transport**
-
SNAPS
- facilitate release of SNAREs for recycling
-
-
chromosome numbers thru meiosis
46(4n)-> meiosis 1-> 23(2n)-> meiosis 2-> 23(1n)
|
|