Cell Membranes & Endomembrane System Flashcards

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1
Q

Why are cell membranes needed?

A
  • define boundaries
  • enclose organelles
  • generation of electrical signals
  • cell signalling
  • attachment sites
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2
Q

What is the endomembrane system?

A

Internal membrane delimiting organelles

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3
Q

Features of the lipid bilayer

A
  • made of hydrophilic heads (polar, choline + phosphate + glycerol) and hydrophobic tails (non-polar, fatty acid, contain 14-24 carbons in length, contain cis double bond which effects membrane packing)
  • contains embedded + attached proteins
  • contains cholesterol to establish stability and fluidity of the membrane
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4
Q

Function of lipids in the cell membrane

A
  • 50% of membrane mass
  • self organising, form spherical shapes to protect fatty acid tails
  • form micelles ( 1 layer) when lipids are in low concentration
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5
Q

Cholesterol in cell membranes

A
  • polar hydroxyl heads sit close to polar heads of the bilayer
  • only found in membranes of animal cells
  • affect membrane fluidity:
    At low temperatures, spacing is increased between hydrocarbons, increased fluidity
    At high temperatures, hydrocarbon tails are pulled together, decreased fluidity
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6
Q

How does temperature affect membrane fluidity?

A
  • increased temperature, hydrocarbons are less packed, membrane is more fluid
  • decreased temperature, hydrocarbons are more packed, membrane is less fluid
  • at very low temperatures the membrane can enter a crystalline state
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7
Q

Other factors affecting membrane fluidity

A
  • lateral movement - phospholipids rapidly moving laterally within the plane
  • flip-flopping - movement of phospholipids between planes (very rare)
  • rotation of phospholipids
  • flexion - movement of hydrocarbon tails
  • cis double bonds - unsaturated, more spread out as chains are more difficult to pack
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8
Q

What are lipid rafts?

A
  • areas enriched with cholesterol and sphingolipids form rafts and move laterally - can pick up proteins
  • means that not all areas of the membrane have the same mobility
  • roles include cell signalling + uptake of extracellular molecules
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9
Q

What is the nuclear envelope and what are its functions?

A
  • contains and inner and outer lipid bilayer
  • controls what enters and exits the nucleus via the nuclear pores
  • selective movement in and out
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10
Q

What are nuclear pore complexes (NPCs)

A
  • embedded in the membrane of the nucleus
  • bidirectional movement
  • octagonal symmetry
  • 3000-4000 per cell
  • transport 500 macromolecules per second
  • Movement in = DNA & RNA building blocks, molecules to provide energy, ribosomal proteins
  • Movement out = ribosomal subunits, synthesised by nucleolus
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11
Q

Nuclear localisation signal (NLS) & nuclear export signal (NES)

A
  • NLS = amino acid sequence that tags a protein fir entry to the nucleus
  • NES = amino acid sequence that tags a protein for exit from the nucleus
  • both recognised by NPCs
  • small proteins move freely
  • larger proteins move slower
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12
Q

Features of the endoplasmic reticulum

A
  • Rough - protein synthesis in ribosomes
  • smooth - lipid synthesis
  • storage of Ca2+ - involved in cell signalling
  • hormone production
  • conversion of glycogen to glucose
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13
Q

Co - translational protein import to ER

A
  • ribosome bound to ER membrane
  • protein imported to ER lumen as it is translated
  • transmembrane proteins are only partially translocated across the membrane
  • water soluble proteins fully translocate across the membrane
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14
Q

After co - translational import to ER
IN ER:

A

IN ER:
- mRNA bound by ribosome
- 2 ribosomal subunits bind together then to mRNA
- complex then binds to translocation machinery embedded within the ER
- ribosome moves along the mRNA, translating it, making 1 amino acid at a time (continuous signal allows the protein to pass through as it is being translated)

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15
Q

Co - translational protein import
IN OTHER STRUCTURES e.g. mitochondria
(POST TRANSLATIONAL)

A

IN OTHER STRUCTURES:
- Ribosome binds to mRNA
- translates it to a protein
- different signal sequence which also binds, allowing the protein to pass through
- signal sequence is cleaved off once protein has been transported

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16
Q

Co - translational translocation into ER

A
  • requires an ER signal sequence
  • large + small ribosomal subunits come together and bind to mRNA bound
  • complex can then interact with translocator complex (closed until ribosome binds)
  • protein passes through translocator until fully made, signal sequence is then cleaved off by signal peptidase
  • mature polypeptide chain is then released into the ER lumen
  • ribosome released and translocator closes
17
Q

Polysomes

A
  • a single mRNA can be simultaneously bound by several ribosomes at a time
  • sucrose gradient separates mRNA with different numbers of attached ribosomes
18
Q

Protein glycosylation in ER

A
  • glycosylation = the addition of complex sugars to proteins to give them different functions
  • lipid linked sugar anchored in membrane interacts with enzyme causing the sugar to be cleaved from the lipid and added onto the protein
  • side chain sugars are added/removed/trimmed in the Golgi
19
Q

Features of the Golgi apparatus

A
  • major site of carbohydrate synthesis e.g. pectin in plants and glycosaminoglycans in animals
  • further glycosylation of proteins
  • plays part if the secretory pathway - sorts and dispatches proteins made in the ER
  • made of interconnected, flattened cisternae
  • cis face + trans face through medial cisternae
20
Q

Movement from ER to Golgi

A
  • bidirectional movement
  • vesicles labelled with COPII proteins which act as signals and direct them from ER to the Golgi
  • COPI protein directs vesicles back to the ER e.g. if incorrectly folded
21
Q

Movement from CIS Golgi to ER

A
  • proteins that should be in ER have KDEL at the end
  • COPII vesicles shed COPII coat and fuse to vesicular tubular clusters, then fuse with CIS Golgi
  • within the Golgi there are KDEL receptors which retrieve the protein and send it back to the ER
22
Q

2 mechanisms for movement of proteins through Golgi

A

1) Cisternal Maturation - cis face of Golgi matures and becomes the trans face, taking the proteins with it
2) Vesicles transport - budding off of vesicles from Golgi which transport proteins as they bind to the next cisternae

  • could be both mechanisms
23
Q

Complex glycosylation of proteins in Golgi

A
  • different enzymes are found in different parts of the Golgi - all have different roles in glycosylation
  • sequence of amino acids determines what happens to the protein and what it is like after glycosylation