chapter 12 intracellular compartments and protein sorting 張學偉 助理教授
TRANSCRIPT
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Chapter 12
• Intracellular Compartments and Protein Sorting
張學偉 助理教授
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The compartmentalization of cells
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All eucaryotic cells have the same basic set of membrane-enclosed
organelles
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The major intracellular compartments of an animal cells.
Cytoplasma = cytosol + cytoplasmic organelles
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The topological relationships of membrane-enclosed organelles
can be interpreted in terms of their evolutionary origins
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Protein can move between compartments in different ways
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Sorting signal by signal sequences
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Vesical transport
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Signal sequences and signal patches direct proteins to the
correct cellular address
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Sorting signal (signal sequences) recognize by sorting receptors
Cut by signal peptidases
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Red +Green -Yellow HydrophobicBlue hydroxylated
N-terminal signalC-terminal signal
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The transport of molecules between the nucleus and the
cytosol
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Nuclear pore complexes perforate the nuclear envelope
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Composed by more than 50 different proteins called nucleoporins.
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9nm
26nm15nm
size
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Nuclear localization signals (NLS) direct nuclear proteins to the
nucleus
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Colloidal gold spheres coated with peptides containing NLS
Nuclear pore transport (large aqueous pore) is fundmental different from organelle transport (lipid bilayer).
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Nuclear import receptors bind nuclear localization signals and
nucleoporins
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FG-repeat (Phe-Gly) serve as binding sites for the import receptors.
Solublecytosolicprotein
Nuclear import do not always bind to nuclear proteins directly.
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Nuclear export works like nuclear import, but in reverse
Nuclear export signals & nuclear export receptor & nuclear transport receptor (karypherins)
tRNA or 5S RNA: nuclei cytosolNLS-particle: cytosol nuclei
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The Ran GTPase drives directional transport through
nuclear pore complexes
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Ran = GTPaseGAP = GTPase-activing proteinGEF = Guanine exchange factor
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Bidirectional model
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Transport between the nucleus and cytosol can be regulated by
controlling access to the transport machinery
Always in & out, shuttling
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Ventral side Dorsol protein
The control fly embryo development by nuclear transport
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The nucleus envelope is disassembled during mitosis
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Lamina (whole structure) & lamins (protein subunit)
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The transport of proteins into mitochondria and chloroplasts
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Newly mito & chloropl are produced by the growth of preexisting organelle.Their growth depends mainly on the cytosolic protein import
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Translocation into the mitochondrial matrix depends on a
signal sequence and protein translocators
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Red = +Yellow = nonpolar
On different side
Amphipathic helix
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translocase
Require for import all nucleus-encoded mitochondria protein
Insert to inner memb.Transport to matrix
For protein synIn mito
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Mitchondrial precursor proteins are imported as unfolded
polypeptide chains
Interacting protein: eg Charperone protein hsp70 family
All Interacting protein help to prevent aggregation before engaging with TOM complex in outer mito membrane.
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Mitochondrial precursor proteins are imported into the matrix at contact sites that join the inner
and outer membranes
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Protein import by mitochondria
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ATP hydrolysis and a H+ gradient are used to drive protein import
into mitochondria
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pulling
Freely permeable to ions and metabolitesbut not to most protein
Charperone protein also function as translocator
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Repeated cycles of ATP hydrolysis by mitochondrial Hsp70
complete the import process.
Hsp 60 provide chamber for unfolded polypeptide chain facilitates folding (chapter 6)
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Protein transport into the inner mitochondrial membrane and the intermembrane space required
two signal sequences
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Two signal sequences are required to direct proteins to the
thylakoid membrane in chloroplasts
Resemble in mitochondria
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peroxisomes
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Peroxisomes use molecular oxygen and hydrogen peroxide to
perform oxidative reactions
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Catalase: 2H2O2 2H2O + O2Urate oxidase: RH2 + O2 R + H2O2
Animal: -oxidation occur at both mitochondria & perixosome.
Plant & yeast: -oxidation occur only at perixosome.
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Plasmalogen-the most abundant protein in myelin.- deficient result in neurological disease.
Animal Perxisome catalyze the first step for plasmalogen biosyn
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Glyoxylate cycle
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A short signal sequence directs the import of proteins into
peroxisomes
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Peroxins:-at least 23 distinct proteins for driving ATP hydrolysis-deficent result in Zellweger syndrome.
Most peroxisomal membrane proteinsare made in the cytosol insert into preexisting peroxisomes.
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The endoplasmic reticulum
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Membrane-bound ribosomes define the rough ER
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Many ribosomes bind to a single mRNA
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ER capture 2 type of protein: transmembrane protein & water-sol protein
Cotranslatioal transport?Posttranslational transport?
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p690
In mammalian cellsProtein import to ER Cotranslational process (chaperone are not required to keep protein unfolded)Protein import to mitochondria, chloroplasts, nuclei, peroxisomes Postranslational process (chaperone needed for unfolding)
Compared to page 697
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Smooth ER abundant in some specialized cells
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Lipid metabolism (cholestersol)Detoxification by cytochrome p450Sequester Ca+2 from cytosol (SR)
Autophagocytosis & phenobarital
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Rough and smooth regions of ER can be separated by
centrifugation
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Cell-free system
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Signal sequences were first discovered in proteins imported
into the rough ER
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A signal-recognition particle (SRP) directs ER signal sequences to a specific receptor in the rough ER
membrane
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ER & SRP for import
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The polypeptide chain passes through an aqueous pore in the
translocator
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Translocation across the ER membrane does not always
require ongoing polypeptide chain elongation
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p693
rare
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yeast
ATPase
Binding protein(hsp70-like chaperone protein)
Protein that areare first released into cytosol (bind to hsp to prevent folding)
c/o sealing the pore
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The ER sequence is removed from most soluble proteins after
translocation
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Start-transfer signal
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In single-pass transmembrane proteins, a single internal ER
signal sequence remains in the lipid bilayer as membrane-
spanning of a helix
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Combinations of start-transfer and stop-transfer signals determine
the topology of multipass transmembrane proteins
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hydrophobicity
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Translocated polypeptide chains fold and assemble in the lumen of
the rough ER
Important ER resident proteins: PDI (protein disulfide isomerase; produce -s-s-)BiP chaperone protein (prevent aggregate & help to keep in ER)
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Most (Soluble & membrane-bounded) proteins synthesized in the RER are glycosylated by the addition of a common N-linked
oligosaccharide
Very few protein in cytosol is glycosylated.
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N-linked oligosaccharide - are by far the most common oligosaccharides found in glycoprotein. (RER)-are recognized by 2 ER charperon protein (calnexin & calreticulin)
O-linked oligosaccharide are found in Golgi.
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Oligosaccharides are used as tags to mark the state of protein
folding
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Improperly folded proteins are exported from the ER and
degraded in the cytosol
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deglycosylation
Retrotranslocation(dislocation)
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Misfolded proteins in the ER activate an unfolded protein
response
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Some membrane proteins acquire a covalently attached
glycosylphosphatidylinositol (GPI) anchor
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Segregate protein from other membrane protein
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Most membrane lipid bilayers are assembled in the ER
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Phospholipid exchange proteins help to transport phospholipids
from the ER to mitochondria and peroxisomes
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1. Roadmap of protein traffic2. Signal sequences & organelle targeting3. Organelle epigenetic control
4. Nuclear pore complex & nuclear import/export & its receptor/signal5. The control of nuclear import during T-cell activation
6. Protein translocation process in mitochondrial membrane: TOM, TIM, OXA7. Relationship among import of mitochondrial precursor proteins, role of energy,its
hsp70.8. Translocation of a precursor protein into the thylakoid space of chloroplasts.
9. Peroxisomal enzymes & reactions, import mechanism distinct from mitochondria & chloroplast or unique character of peroxisome
10. SER, RER preparation, SRP, ribosome and RER protein transport11. Cotranslation & postranlation translocation in bacteria, archea, and eucaryotes12. Hydrophobicity of membrane protein and transmembrane domain13. Process and role of protein N-link glycosylation in RER14. Membrane lipid bilayer assembly in ER: using example of phosphatidylcholine
synthesis15. Phospholipid transport from ER to other organelles and comparison of ER and plasma membrane
Chapter 12 practice