TAMU BIOL 213 - Protein Modification in the ER, Endocytosis, & Exocytosis (8 pages)

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Protein Modification in the ER, Endocytosis, & Exocytosis



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Protein Modification in the ER, Endocytosis, & Exocytosis

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Lecture number:
20
Pages:
8
Type:
Lecture Note
School:
Texas A&M University
Course:
Biol 213 - Molecular Cell Biol
Edition:
1

Unformatted text preview:

BIOL 213 1st Edition Lecture 20 Outline of Last Lecture I The fate of proteins after synthesis compartmentalization II Protein sorting a Necessary and sufficient III Transport through nuclear pores IV Transport across membranes a Mitochondria and chloroplast b ER membrane i Soluble proteins ii Transmembrane proteins V Transport by vesicles a Highly specific Outline of Current Lecture I Protein modification in the ER a Disulfide bond formation b Glycosylation II Exit of proteins from the ER is controlled a Chaperones hold onto misfolded proteins III Protein modification and sorting in the Golgi These notes represent a detailed interpretation of the professor s lecture GradeBuddy is best used as a supplement to your own notes not as a substitute a Glycosylation and other signal sequences on the cargo proteins tell the vesicles where to go IV Exocytosis a Constitutive exocytosis pathway i Continuous b Regulated exocytosis pathway i Ex neurotransmitters V Endocytosis a Phagocytosis eating i Really large molecules like bacterial cells b Pinocytosis drinking i Smaller molecules ii Indiscriminate pinocytosis 1 Continuous iii Receptor mediated endocytosis 1 Ex cholesterol VI Lysosomes a Three different pathways to a lysosome Current Lecture I Protein modification in the ER a Disulfide bond formation i The ER lumen is an oxidizing environment meaning it will cause atoms to lose electrons electron density 1 The cytosol is a reducing environment ii This causes disulfide bridges to form between the side chains of amino acids because a sulfur bonded to a sulfur is more oxidized than a sulfur bonded to a hydrogen iii This stabilizes the protein b Glycosylation i This is when a 14 sugar oligosaccharide is added to a protein ii The main one we study is the N linked side group iii This is the attachment of the 14 sugar oligosaccharide to an asparagine 1 Before it s attached to the protein it s bonded to dolichol in the ER membrane a Dolichol is a transmembrane lipid with two



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