11 MZB I - Devuyst 2
Intracellular compartments an transport
Intracellular compartments an transport
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Lernkarten
mtDNA
-> codiert für (wieviel)
Fachsprachlich wird als mitochondriale DNA, kurz mtDNA, die zumeist zirkuläre, doppelsträngige DNA im Inneren (Matrix) der Mitochondrien bezeichnet.
-> in humans, the over 16000 base pairs of mitochondrial DNA encode for only 37 genes: 13 for Proteins, 22 for Transfer RNA
MELAS
Mitochondrial Encephalopathy, Lactic Acidosis and Stroke-like episodes (MELAS)
Als MELAS-Syndrom bezeichnet man eine mitochondriale Enzephalomyopathie
Golgi apparatus:
Zweck
Synthesis, packaging, routing of proteins
• Stacks of membrane-enclosed sacs
• Reception, modification and routing of proteins made in ER
• Surrounded by small vesicles (in – out traffic)
Lysosomes:
Zweck
Intracellular digestion, garbage
• Lysosomes break down cellular waste products and macromolecules into simple compounds, which are then transferred back into the cytoplasm as new materials.
• To accomplish the digestion lysosomes utilize 40 different types of hydrolytic enzymes, which are manufactured in endoplasmic reticulum and modified in the Golgi.
Peroxisomes:
Zweck
Degradation of hydrogen peroxide
• Peroxisomes contain enzymes that convert (cytotoxic) hydrogen peroxide to water (oxidative
lysosomes reactions).
• Were first discovered by the Belgian scientist Christian de Duve, who also discovered y
sorting signals
KDEL
The fate of proteins synthesized in cytosol depends on the AA sequence → sorting signals to direct proteins into nucleus/organelles/ER
KDEL is a target peptide sequence in the amino acid structure of a protein which prevents the protein from being secreted from the endoplasmic reticulum (ER). A protein with a functional KDEL motif will be retrieved from the Golgi apparatus by retrograde transport to the ER lumen.
- K—Lysine
- D—Aspartic acid
- E—Glutamic acid
- L—Leucine
Lys-Asp-Glu-Leu.
Fatty acid acylation
"Fatty acid acylation is the covalent attachment of fatty acids to proteins."
• Protein acylation is a post-translational modification of proteins.
• Prominent type: fatty acylation, the addition of fatty acids to particular amino acids (e.g. myristoylation or palmitoylation)
• Protein acylation is a mechanism of biological signaling
mechanism signaling
-> Die Kopplung von Fettsäuren wie Myristinsäure oder Palmitinsäure führt zur Bindung der acylierten Proteine an die Zellmembran. Dieser Prozess kann für die Funktion des gesamten Proteins von großer Bedeutung sein.
Prenylation
Prenylation (also known as isoprenylation or lipidation) is the addition of hydrophobic molecules to a protein or chemical compound. It is usually assumed that prenyl groups (3-methyl-but-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence is missing.
• Addition of hydrophobic molecules to a protein
• Facilitate attachment to cell membranes
Secretory pathway
Ursprung/ ziel
The secretory pathway is a series of steps a cell uses to move proteins out of the cell, a process known as secretion. The path of a protein destined for secretion has its origins in the rough endoplasmic reticulum, a membrane-bound compartment in the cell. The protein then proceeds through the many compartments of the Golgi apparatus and finally ends up in a vesicle that transiently fuses at the cell plasma membrane via permanent plasma membrane structures called porosomes, depositing the proteins on the outside of the cell.
Transfer of Proteins from Cytosol to ER:
Signal sequence
- what kind of AAs are in this sequence?
Common Pool of Ribosome Subunits
A common pool of ribosomes is used to synthesize the proteins that stay in the cytosol and those that are transported into the ER. The ER signal sequence on a newly formed polypeptide chain directs the engaged ribosome to the ER membrane. The mRNA molecule remains permanently bound to the ER as part of a polyribosome, while the ribosomes that move along it are recycled; at the end of each round of protein synthesis, the ribosomalsubunits are released and rejoin the common pool in the cytosol.
"Passage" von mRNA durch den Translocation Channel
Ablauf/prinzip
• Signal sequence: opens the translocation channel • Rest of the protein threaded across the membrane (loop)
• Recruitment of a signal peptidase
→ cleavage of signal peptide, degraded
→ translocated peptide soluble in ER lumen,
→ Pore of the channel closed
(On binding an ER signal sequence (which acts as a start-transfer signal), the translocator opens its pore, allowing the transfer of the polypeptide chain across the lipid bilayer as a loop. After the protein has been completely translocated, the pore closes, but the translocator now opens laterally within the lipid bilayer, allowing the hydrophobic signal sequence to diffuse into the bilayer, where it is rapidly degraded.)
Topologie von Membranproteinen:
Different types of anchor sequences (I, II,III)
stretch of positively-charged AA
Internal signal-achor
Stop-transfer anchor
• Stretch of positively‐charged AA :
• Always cytosolic side
• Always associated with signal‐anchor
• Internal signal‐anchor (SA) : always associated with positive stretch of AA
• Positive stretch can be on both sides of the SA
• Stop‐transfer anchor (STA) : hydrophobic ‐ always stop translocation
• Transition between ER lumen and cytosol
• Never associated with positive stretch of AA
Topology of ER Membrane Proteins:
Type IV (A und B):
Wie werden diese Proteine durch die Membran verankert?
• Internal hydrophobic signal anchor (SA) sequence, with +++ strech on cytosol side
• Translocation continues until stop‐transfer anchor (STA) sequence
→ Transmembrane proteins with a‐helices: Type IV – paired signals
(an internal ER signal sequence acts as a start-transfer signal and initiates the transfer of the C-terminal part of the protein. At some point after a stop-transfer sequence has entered the translocator, the translocator discharges the sequence laterally into the membrane.)
Multipass Membrane Protein: Rhodopsin
Rhodopsin is a pigment of the retina, responsible for the formation of photoreceptors cells and the light perception.
(Rhodopsin is the light-sensitive protein in rod photoreceptor cells in the mammalian retina (discussed in Chapter 15). (A) A hydrophobicity plot identifies seven short hydrophobic regions in rhodopsin. (B) The most N-terminal region serves as a start-transfer sequence that causes the preceding N-terminal portion of the protein to be passed across the ER membrane. Subsequent hydrophobic sequences function in alternation as start-transfer and stop-transfer sequences. (C) The final integrated rhodopsin has its N-terminus located in the ER lumen and its C-terminus located in the cytosol. Theblue hexagons represent covalently attached oligosaccharides. Arrows indicate the parts of the protein that are inserted into the translocator.)
GlycosylPhosphatidylInositol‐Anchor (GPI)
Glykosylphosphatidylinositol-Anker, kurz GPI-Anker, steht für eine kovalente Verknüpfung des membranständigen Phospholipids Phosphatidylinositol an das C-terminale Ende eines Proteins mithilfe einer Glykankette.
-> Glycolipid attached to the C‐terminus of a protein (post‐translational modification)
-> Two fatty acids anchor the protein to the membrane
GPI Anker:
Bildung von GPI‐verankerten Membranproteinen
• Signal peptide o the ER
• C-term hydrophobic – in the membrane
• Hydrophobic end : cleaved off and replaced by the GPI-anchor
• Transfer to Golgi into vesicles and to extracellular space: attached to external leaflet
(Immediately after the completion of protein synthesis, the precursor protein remains anchored in the ER membrane by a hydrophobic C-terminal sequence of 15–20 amino acids; the rest of the protein is in the ER lumen. Within less than a minute, an enzyme in the ER cuts the protein free from its membrane-bound C terminus and simultaneously attaches the new C terminus to an amino group on a preassembled GPI intermediate)
Uromodulin (Tamm–Horsfall protein):
Release (of Uromodulin) from the membrane
Uromodulin (Tamm-Horsfall-Protein) ist ein Protein, das von der Niere in den Urin ausgeschieden wird.
Uromodulin wird via Glycosyl-Phosphatidyl-Inositol (GPI) an die luminale Zellmembran transportiert. Dort wird es proteolytisch gespalten und in das Lumen des Nierentubulus freigesetzt.
-> Cleavage of the group by phospholipases → controlled release of the protein from the membrane
Post-translational Modification in the ER:
Chemical modifications
Most proteins that enter the ER are chemically modified there:
• Formation of disulfide bonds
• Glycosylation
• Proteolysis
Protein Traffic between ER and Golgi:
direction
Gradient of immature-to-mature protein
• Traffic is unidirectional, from ER to Golgi
•In ER, protein is synthesized and modified
•In Golgi, protein is modified and sorted
• Vesicle traffic to plasma membrane
Formation of Disulfide Bonds in ER
Bedeutung
Katalysator
Richtung der Oxidation/ der Reduktion
welches Nebenprodukt entseht
• Formation of covalent cross-links: sulfur-sulfur bonds (adjacent cysteine side chains)
• Oxidation of cysteine pairs mediated by PDI (protein disulfide isomerase) in ER
• Stabilization of protein structure – resistance to pH & enzymes
(One important ER resident protein is protein disulfide isomerase (PDI), which catalyzes the oxidation of free sulfhydryl (SH) groups on cysteines to form disulfide (S-S) bonds. Almost all cysteines in protein domains exposed to either the extracellular space or the lumen of organelles in the secretory and endocytic pathways are disulfide-bonded)
ER Protein Glycosylation
Function
Häufigkeit
Oligosaccharide side chains (sugars) added to proteins in the ER, producing glycoproteins
-> "putting clothes of sugar around the protein"
-> Enzymes present in ER (NOT in cytosol)
Functions of glycosylation:
- Protection from degradation (e.g. proteins in lysosomes)
- Transport and packaging signals
- Cell recognition: displayed on outer membrane as glycocalyx - Cell-cell interactions, receptors, signal transduction, adhesion, …
> 50 % of human proteins are glycosylated
> 1 % of our genes are involved in glycosylation
ER Protein Glycosylation:
Oligosaccharide Attachment
To which AA (and which AA sequence) is the olligosaccharide added?
Dolichol
oligosaccharid; wie sieht der aus?
• Addition of oligosaccharides to Asn (N)
• Sequences: N‐linked
Asn – X – Ser
Asn – X – Thr
The precursor oligosaccharide is held in the ER membrane by a special lipid molecule called dolichol, and it is transferred to the target asparagine in a single enzymatic step immediately after that amino acid has emerged into the ER lumenduring protein translocation
The Proteins Are Glycosylated by the Addition of a Common N-linked Oligosaccharide
-> All of the diversity of the N-linked oligosaccharide structures on mature glycoproteins results from the later modification of the original precursor oligosaccharide.
Glycolisation of proteins in the ER:
Formation of the Core Oligosaccharide on Dolichol Phosphate
The precursor oligosaccharide is linked to the dolichol lipid by a high-energy pyrophosphate bond, which provides theactivation energy that drives the glycosylation reaction. The entire precursor oligosaccharide is built up sugar by sugar on this membrane-bound lipid molecule before its transfer to a protein. The sugars are first activated in the cytosol by the formation of nucleotide-sugar intermediates, which then donate their sugar (directly or indirectly) to the lipid in an orderly sequence. Partway through this process, the lipid-linked oligosaccharide is flipped from the cytosolic to the lumenal side of the ER membrane
Glycolisation of proteins in the ER:
Transfer of glycosilated proteins to Golgi;
what happens to the olgigosacharide linkedto the protein befor its transfer to the golgi?
While still in the ER, three glucoses and one mannose are quickly removed from the oligosaccharides of most glycoproteins.
-> After cleavage of 3 glucose and 1 mannose residues, the protein is transferred to the Golgi.
O-linked glycosylation
when/where does it take place
role
(It is not only the N-linked oligosaccharide chains on proteins that are altered as the proteins pass through the Golgi cisternae en route from the ER to their final destinations; many proteins are also modified in other ways. Some proteins have sugars added to the OH groups of selected serine or threonine side chains. This O -linkedglycosylation, like the extension of N-linked oligosaccharide chains, is catalyzed by a series of glycosyl transferase enzymes that use the sugar nucleotides in the lumen of the Golgi apparatus to add sugar residues to a protein one at a time.)
• It refers to the attachment of glycans to O in lateral chain o
• O‐linked glycosylation of secreted and membrane bound proteins is a post‐translational event that takes place in cis‐Golgi compartment after N‐glycosylation and folding.
• O‐linked glycans play important roles in protein localization and trafficking, protein solulbility and cell-cell interactions