Protein Trafficking Flashcards

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1
Q

Pathways cells use to moves proteins across plasma membrane

A

Carrier proteins, channels, endocytosis (caveolae-mediated, receptors, receptor-mediated), exocytosis, phagocytosis, transcytosis

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2
Q

Carrier proteins

A

Bring proteins across the membrane that cannot simply diffuse

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3
Q

Channel proteins

A

Allows the protein to enter when given the signal to

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4
Q

Caveolae-mediated endocytosis

A

Pit lined with caveolin brings molecules in a membrane bound vesicle

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5
Q

Receptor-mediated endocytosis

A

Bound receptors in coated pits get encircled by coated vesicle

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6
Q

Exocytosis

A

Early endosome is at a low pH, late endosome fuses with a lysosome to break down material and then fuses with a phagosome to dispose of the material

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7
Q

Phagocytosis

A

Microbe is encapsulated and combines with lysosome to create phagolysosome, and digested material is released

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8
Q

Transcytosis

A

Molecules are brought into the cell via vesicle, then released

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9
Q

Bilayer sheet

A

Make up membranes, composed to two sheets, the lipid bilayer

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10
Q

Liposome

A

Spherical lipid bilayers, inside is hollow or filled with liquid

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11
Q

Micelle

A

Spherical, single lipid layer, outside is polar while inside is nonpolar

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12
Q

Channels

A

Use passive diffusion and go with the concentration gradient

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13
Q

Pumps

A

Use active energy-dependent transport and goes agains the concentration gradient

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14
Q

ABC transporters

A

Ligand binds open dimer, ATP binding causes a conformational change that releases the ligand, ATP hydrolyzed and ADP released to open up the dimer again

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15
Q

Nucleus

A

Made up of two lipid bilayers (inner and outer membranes) separated by perinuclear space (lumen). Membranes have nuclear pores

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16
Q

How do proteins enter the nucleus?

A

Small proteins can just diffuse in, but larger proteins need a nuclear localization signal bound to get through the nuclear pore

17
Q

ER/Golgi membrane protein trafficking pathway

A

Proteins co-translationally inserted into RER through translocons, packaged into vesicles in RER, vesicles take proteins to Golgi, where the proteins are sorted and sent to either the lysosome, plasma membrane, or secretory vesicle

18
Q

Misfolded/unfolded proteins

A

Chaperone takes protein to an ER protein translocator and takes into cytoplasm where ubiquitin tags it and sends to the proteosome, which degrades it into small peptides and amino acids to be recycled

19
Q

Lysosome function

A

To degrade macromolecules and cells using internal low pH and acid hydrolases

20
Q

Lysosome storage diseases

A

Tay-Sachs, Guacher’s, metachromatic leukodystrophy
Caused by mutations in lysosome that prevent breakdown of damaged proteins, so these proteins are stored when they shouldn’t be

21
Q

Cystic fibrosis

A

Caused by mutation in CFTR gene where there is no Ca2+ channels on the epithelial cells, leading to dehydration of tissues and mucous

22
Q

Botulism

A

Blocks SNARE interactions so neurotransmitters are released by the presynaptic cell, but cannot be taken up by the post-synaptic cell. Causes autonomic system to fall apart.