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Fig. 1.11
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Nucleus: structure and function
Heterochromatin = too compacted, transcriptionally inactive nuclear envelope Nucleolus Nucleoplasm Euchromatin = can be transcriptionally active
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Nuclear envelope and lamina
cytoplasm N. lamina Nuclear pore heterochromatin
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Nuclear lamina
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Lamins are filamentous proteins in the intermediate filament family
Lamin phosphorylation in prophase disassembles the nuclear lamina & allows for nuc. envel. breakdown Laminins are extracellular proteins, unrelated
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Nuclear pore nuclear localization signals (nuclear import signals)
nuclear export signals highly regulated
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Mitochondria(on) outer membrane DNA inner membrane matrix cristae
ribosomes ATP synthase
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Inner Membrane and matrix
hi [H+] electron transport system ATP synthase FADH2 NADH Krebs cycle ATP4- Antiporter ADP3- symporter pyruvate P04-2 H+
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Endosymbiotic theory: Mitochondria are similar to prokaryotes
Own circular, naked DNA Own ribosomes - similar to prokaryotic e.g. sensitive to same inhibitors Divide by fission Double membrane suggests endocytosis
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Lysosomes: membranous organelles filled with digestive enzymes
Breakdown endocytosed materials Thru’ phagocytosis or receptor mediated endocytosis Breakdown old organelles (residual body) Acidic pH
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Phagocytosis vs. Autophagy
lysosomes Autophagy
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Membrane trafficking RER to cis Golgi
Modified in Golgi (glycosylation, phosphorylation) Sorted at trans Golgi network into Lysosomal Regulated constitutive
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Rough endoplasmic reticulum
Ribosomes Synthesis of secreted and membrane proteins
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Rough Endoplasmic reticulum
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Signal hypothesis: signal peptide, SRP, SRP-receptor, translocon
SRP = signal recognition particle
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Smooth ER, lipid synthesis, detox, Ca2+ sequestration
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Golgi
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Transport thru’ Golgi cisternae is vectorial
Medial Trans
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Protein modifications occur in steps in the Golgi
Protein modifications occur in steps in the Golgi. The extent of changes varies. CIS & CGN RER retrieval, PO4 on mannose, mannose removal mannose removal N-acetylglucosamine addition MEDIAL fucose and glucose addition TRANS sialic acid addition, sorting TGN
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Glycosylation Karp, Fig. 8.20
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Sorting at the TGN constitutive secretion lysosomal pathway regulated
trans Golgi network
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Receptor Mediated endocytosis
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Plasma membrane & Fluid mosaic model
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Phospholipids are most common in membranes
Polar Head Fatty acid tails
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phospholipids, glycolipids, and cholesterol
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Thermodynamics drives membranes to form sealed compartments
Cut open liposome H2O
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Fluidity means that lipids (& proteins) can “float” in the membrane via diffusion
Time
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Three classes of membrane proteins: Transmembrane proteins (a type of IMP)
Oligosaccharides - always face out Extracellular domain (ECD) OUT Transmembrane domain Intracellular domain (ICD) IN
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Three classes of membrane proteins: Lipid-anchored membrane proteins (IMPs)
Covalently linked to a glycophospholipid. E.G.: Normal cellular scrapie protein & alkaline phosphatase OUT Covalently linked to fatty acid IN E.G.: ras
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Three classes of membrane proteins: Peripheral membrane proteins (PMPs)
OUT IN Or, PMPs could bind to specific lipid heads. Specific interaction between IMP & PMP
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IMPs as -helix or -barrel
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Selective permeability
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Osmosis causing cell lysis.
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Four mechanisms by which solute molecules move ACROSS membranes
Simple diffusion across bilayer Simple diffusion thru channel Facilitated Diffusion thru’ passive transporters Active transport
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Membrane Potential Affects Molecular Movement
A. neutral No effect on inward transport No effect on outward transport B. cation Favors inward transport Opposes outward transport C. anion Opposes inward transport Favors outward transport
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Passive transport by channel proteins: don’t bind solute & can be ligand-, voltage-, or stress-gated
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Passive Transport by Facilitated diffusion
Solute binds transporter protein So, transport is saturable
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Kinetics of carrier-mediated transport
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Active transport by the Na/K pump or ATPase
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