11 MZB I - Devuyst 2

Intracellular compartments an transport

Intracellular compartments an transport


H. M.
Diese Lernkarten behandeln auf Universitätsniveau die zellulären Transportmechanismen, insbesondere die receptorvermittelte Endozytose, den vesikulären Transport und die Rolle des Golgi-Apparats. Sie konzentrieren sich auf Prozesse wie die Aufnahme von Proteinen, die Sortierung in Vesikeln und die Fusion von Membranen, wobei Schlüsselkomponenten wie Clathrin, SNARE-Proteine und Rab-Proteine eine zentrale Rolle spielen. Diese Lernkarten sind besonders nützlich für Medizinstudenten, die ein tiefes Verständnis der zellulären Mechanismen und ihrer klinischen Relevanz, wie bei der familiären Hypercholesterinämie, erlangen möchten.
Flashcards
68
Students
8
Language
German
Category
Medical
Level
University
Created / Updated
11.05.2016 / 10.06.2018

Flashcards

Wozu ist glycolisation von Proteinen nötig?

- Numerous proteins depend on glycolisation for their uniwue functions such as proteoglycans which are requierrs to fotma fully functional extracellular matrix.
- Other proteins, such as acid hydrolases, rely on modified N-glycosyl groups for the targeting of the protein to the lysosome.

Congenital Disorders of glycosylation:

(molecular) reason

CDG bedeutet Congenital Disorders of Glycosylation, was wörtlich übersetzt angeborene Erkrankungen der Glykosylierung bedeutet.

A Defect in Dolichol Phosphate Biosynthesis Causes a New Inherited Disorder with Death in Early Infancy

Preproisulin processing in ER

Preproinsulin is the primary translational product of the INS gene.

• Food intake: insulin mRNA is translated as a single chain preproinsulin (110 AA) in the pancreas.
• Removal of its signal peptide during insertion into the endoplasmic reticulum, proinsulin is generated (disulfide bonds)
• Within Golgi, proinsulin is exposed to endopeptidases to excise the C peptide chain of 31 amino acids to derive insulin.
• Mature insulin has been made into clusters of endocrine cells in inslets of Langorhans.
• Once beta cell is appropriately stimulated, insulin is secreted from the cell into the blood.

Exit of Proteins from ER & Protein Quality

chaperones

Most proteins that enter ER are bound to other locations:
  -> Vesicles, budding and fusing with Golgi, …

Exit from ER is selective: misfolded proteins are retained in ER 
  -> Binding to chaperones until proper folding
     -> If no proper folding: degradation

=> ER controls the quality of proteins exported to Golgi

What happens to misfolded Proteins in the ER?

Export and degradation of misfolded ER proteins

(Als Ubiquitinierung bezeichnet man die Übertragung von Ubiquitin auf ein Zielmolekül. Die Folge ist in den meisten Fällen der Abbau im Proteasom.)

Cystic Fibrosis:

Häufigkeit

molecular cause

Most common lethal genetic disease in Caucasians
  - Prevalence: 1:2,500 (carriers 1:25)
  - Lifespan reduced to ~30 years

CFTRmutations cause Cystic Fibrosis

Unfolded Protein Response

Als Unfolded Protein Response (UPR, dt. ungefaltete Proteinantwort oder Antwort auf ungefaltete Proteine) wird in derBiologie eine komplexe Antwort von Zellen auf Stress bezeichnet, der durch die Ansammlung von Proteinen mit fehlerhafterFaltung im endoplasmatischen Retikulum (ER) entsteht.

Transcriptional responseto Accumulation of issfolded Proteins in the ER: Unfolded Protein Response (UPR)
 - Adaptation, increased synthesis of ER machinery (expansion)
 - increased Chaperones

Transport of M6P-containing Proteins :

Where are they transported to?

Where are the tagged witch M6P?

M6P receptors

Transport of M6P-containing Proteins to Lysosomes

• Specialized enzymes of lysosomes : synthesized in ER → Golgi
• In ER and cis-Golgi: enzymes are tagged with mannose-6-phosphate sugar
• Trans-Golgi: M6P recognized by M6P receptor → sorted to lysosomes
• Binding of M6P in trans-Golgi and release in the lumen of lysosome: pH dependent
• M6P receptors are recycled to the trans-Golgi

(The precursors of lysosomal hydrolases are covalently modified by the addition of mannose 6-phosphate (M6P) groups in the cis Golgi network. They then become segregated from all other types of proteins in the trans Golgi network because adaptins in the clathrin coat bind the M6P receptors, which, in turn, bind the modified lysosomal hydrolases. The clathrin-coated vesicles produced bud off from the trans Golgi network and fuse with late endosomes (which later turn into Lysosomes). At the low pH of the late endosome, the hydrolases dissociate from the M6P receptors, and the empty receptors are recycled to the Golgi apparatus for further rounds of transport.)

Mannose 6-phosphate Tagging of Lysosomal Hydrolases

Enzym

In ER and cis-Golgi network:
• The N-glycosyl group is first modified to produce a high mannose-containing oligo.
• Phosphate addition to C6 is catalyzed by N-acetylglucosamine phosphotransferase.
• This enzyme binds to and recognizes a signal patch on the folded hydrolase.
• N-acetyl glucosamine is then removed to produce a mannose-6-phosphate

(The GlcNAc phosphotransferase enzyme that recognizes lysosomal hydrolases in the Golgi apparatus has separate catalytic and recognition sites. The catalytic site binds both high-mannose N-linked oligosaccharides and UDP-GlcNAc. The recognition site binds to a signal patch that is present only on the surface of lysosomal hydrolases. The GlcNAc is cleaved off by a second enzyme, leaving the M6P exposed (not shown).)

Thesaurimoses

molecular cause

Bei einer Thesaurismose (früher Thesaurose) – von griech.: thesaurisma (Schatz, Vorrat) – oder Speicherkrankheit handelt es sich um eine Synthese oder Abbau betreffende Stoffwechselstörung. Jede Krankheit dieser Gruppe verursacht eine Anhäufung eines spezifischen Stoffwechselprodukts mit einem spezifischen Verteilungsmuster im Körper.

Defective lysosomal enzymes or defective targeting:
- Thesaurismoses – Lysosomal Storage Diseases 

Vesicular Transport:

Secretory Pathway
Endocytic Pathway
-> From Where to where

• Secretory pathway: From ER → Golgi → endo/lysosomes or plasma membrane (pink) 
• Endocytic pathway: From extracellular space → lysosomes (green)

Clathrin-coated Vesicles

Origin/Destination

Ablauf

From Golgi – secretory - to lysosome (via endosome)
From plasma membrane - endocytosis - to endosomes

• Cargo receptors – captured by adaptins – bind to clathrin molecules (cytosol)
• Basket network – coated pit – dynamin assembly around the neck of vesicle
• Dynamin (GTPase) – pinch off the vesicle
• Removal of adaptin-coat – naked vesicle to fuse with target membrane

COP proteins

what do they do?

COP Proteins are a type of vesicle coat proteins.
-> COP-coated vesicles most commonly mediate transport between ER and Golgi

Oculo-Cerebro-Renal Syndrome of Lowe

Cause
- molecular
- genetisch

• Caused by mutations in OCRL1
  -> PtdIns(4,5)P2 5-Phosphatase
•X-linkedmultisystemic disorder
  1. Proximal tubular dysfunction (Fanconi Syndrome)
  2. Bilateral congenital cataracts
  3. Severe mental retardation (40 < IQ < 54) .

OCRL1

Distribution

Role

PtdIns(4,5)P2 5-Phosphatase 

• Distribution: Trans-Golgi network (major sorting site)

Role: Modulates the pool of membrane PtdIns(4,5)P2 :
1. Regulation of lysosomal enzymes delivery
2. Regulation of cell junctions and intracellular trafficking

Vesicle Docking:

Rabs and SNAREs

• Specificity of vesicular transport: markers on vesicles – receptors on membrane
• Rab proteins: small GTPases on vesicles – Tethering proteins on membranes
  -> Rab Proteins Help Ensure the Specificity of Vesicle Docking
• Complement: vesicular (v-SNARE) – target membrane (t-SNARE)
  ->SNARE proteins seem to have a central role both in providing specificity and in catalyzing the fusion of vesicles with the target membrane

Vesicle & Membrane Fusion:

SNAREs (v-SNARE nd t-SNARE)

(gorber) Ablauf

(SNARE proteins exist ascomplementary sets—vesicle membrane SNAREs, called v-SNAREs, and target membrane SNAREs, called t-SNAREs. v-SNARESs and t-SNAREs have characteristic helical domains. When a v-SNARE interacts with a t-SNARE, the helical domains of one wrap around the helical domains of the other to form stable trans-SNARE complexes, which lock the two membranes together.)

• Fusion: closer contact than docking - two bilayers within 1.5 nm
• Lipid intermix & water expulsion: high energy required, specific signals
• SNARE complex plays a central role + other proteins

Docking & Fusion of Vesicles:

Welches Protein ist (v.a.) zuständig für
- Identification
- Fusion
- dissociation of SNARE complex

• Identification : Rab proteins
• Fusion : SNARE complexes
• NSF (ATPase) & α‐SNAP: dissociation of SNARE complex

Vesicular Transport from ER to Golgi & Return

Which cat-Proteins are used in either way?

COPI-coated vesicles and COPII-coated vesicles transport material early in the secretory pathway: COPII-coated packages bud from the ER, and COPI-coated packages bud from pre-Golgi compartments and Golgi cisternae.

    GOLGI
COPII proteins ↑
COPI proteins ↓
       ER

TransGolgiNetwork:

Constitutive vs. Regulated Secretory Pathways

-> consituitive Sceretion is not regulated

Beispiele für regulierten sekretorischen Weg:
Hepatozyt, exokrine Zellen, endokrine Zelle, Neurone

(The two pathways diverge in the trans Golgi network. The constitutive secretory pathway operates in all cells. Many soluble proteins are continually secreted from the cell by this pathway, which also supplies the plasma membrane with newly synthesized lipids and proteins. Specialized secretory cells also have a regulated secretory pathway, by which selected proteins in the trans Golgi network are diverted into secretory vesicles, where the proteins are concentrated and stored until an extracellular signal stimulates their secretion)

Endocytosis

phagocytosis/pinocytosis

 

"Uptake of material into a cell by an invagination of the plasma membrane and its internalization in a membrane-bounded vesicle."

Two main types ofendocytosis are distinguished on the basis of the size of the endocytic vesicles formed. One type is called phagocytosis (“cellular eating”), which involves the ingestion of large particles, such as microorganisms or dead cells via large vesicles called phagosomes (generally >250 nm in diameter). The other type is pinocytosis (“cellular drinking”), which involves the ingestion of fluid and solutes via small pinocytic vesicles (about 100 nm in diameter). 

• Endocytosis: Continuous uptake of fluids, large & small molecules
  → Specialized cells: uptake of large particles and cells
• Size of endocytic vesicles:
  * Pinocytosis: small vesicles (< 150 nm)
  * Phagocytosis : large vesicles, phagosomes (>250 nm)

Clathrin vermittelte Endozytose

The endocytic part of the cycle often begins at clathrin-coated pits (Region of plasma membrane of animal cells that is coated with the protein clathrin on its cytosolic face. Such regions are continually forming and budding off by endocytosis to form intracellular clathrin-coated vesicles containing extracellular fluid and the materials dissolved in it.)

Receptor-Mediated Endocytosis:

Prinzip

Zweck

Wo kommt die Receptor-Mediated Endocytosis (als Beispiel) vor?

-> Selective form of pinocytosis that increases the efficiency of internalization of macromolecules

• >1000‐fold more effective than pinocytosis: concentrating mechanism
• Minor components of the ECF can be taken up in large amounts • Clearance of proteins and drugs
• Metabolization of vitamins, iron, hormones, choleterol

Epithelial cells lining the proximal tubule of the kidney

Receptor-mediated Endocytosis:

LDL Receptor
-> Mutations in LDLR lead to

(Most cholesterol is transported in the blood as cholesteryl esters in the form of lipid-protein particles known as low-density lipoproteins (LDL). When a cell needs cholesterol for membrane synthesis, it makes transmembrane receptor proteins for LDL and inserts them into its plasma membrane. Once in the plasma membrane, the LDL receptors diffuse until they associate with clathrin-coated pits that are in the process of forming. Since coated pits constantly pinch off to form coated vesicles, any LDL particles bound to LDL receptors in the coated pits are rapidly internalized in coated vesicles. After shedding their clathrin coats, the vesicles deliver their contents to early endosomes, which are located near the cell periphery. Once the LDL and LDL receptors encounter the low pH in the endosomes, LDL is released from its receptor and is delivered via late endosomes to lysosomes. There the cholesteryl esters in the LDL particles are hydrolyzed to free cholesterol, which is now available to the cell for new membrane synthesis. If too much free cholesterol accumulates in a cell, the cell shuts off both its own cholesterol synthesis and the synthesis of LDL receptor proteins, so that it ceases either to make or to take up cholesterol.)

Mutations LDLR : Familial hypercholesterolemia
= the presence of high levels ofcholesterol in the blood

Receptor-mediated Endocytosis:

Vesicular Acidification
Prinzip

s.B.

Fate of endocytosed proteins
(3 möglichekeiten, knapp)

Three pathways from the endosomal compartment in an epithelial cell are shown. Retrieved receptors are returned (1) to the same plasma membranedomain from which they came (recycling) or (2) to a different domain of the plasma membrane (transcytosis). (3) Receptors that are not specifically retrieved from endosomes follow the pathway from the endosomal compartment to lysosomes, where they are degraded (degradation).

Transzytose

Unter Transzytose versteht man einen rezeptorvermittelten Transport von Substanzen durch Zellen hindurch.

Transport of M6P-containing Proteins from ER to Lysosomes

Prinizp

 

• Specialized enzymes of lysosomes : synthesized in ER → Golgi
• In ER an cis-Golgi: enzymes are tagged with mannose-6-phosphate sugar
• Trans-Golgi: M6P recognized by M6P receptor → sorted to lysosomes
• Binding of M6P in trans-Golgi and release in the lumen of lysosome: pH dependent
• M6P receptors are recycled to the trans-Golgi

=(The precursors of lysosomal hydrolases are covalently modified by the addition of mannose 6-phosphate (M6P) groups in the cis Golgi network. They then become segregated from all other types of proteins in the trans Golgi network because adaptins in the clathrin coat bind the M6P receptors, which, in turn, bind the modified lysosomal hydrolases. The clathrin-coated vesicles produced bud off from the trans Golgi network and fuse with late endosomes. At the low pH of the late endosome, the hydrolases dissociate from the M6P receptors, and the empty receptors are recycled to the Golgi apparatus for further rounds of transport.)

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