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Golgi, morphologically and biochemically different - Coggle Diagram

- - - - N-linked glycosylation
        
        Sugar residues are trimmed, making the protein active
        and more specific
      - O-linked glycosylation
        
        A sugar residue is added to a hydroxy (-OH) group in
        the protein
        
        Two amino acids can be added to make it active:Threonine and serine
    - - Sugar residues have “mannose” at the end
      - when mannose is phosphorylated, liposomal enzymes are activated, and the protein is tagged for lysosomal degradation
- - - - faces the RER
        
        this siide receives the vesicles from the RER, which are covered in two possible types of proteins
        
        COP-I
        
        This COP is responsible for making the vesicles come back to the RER from the Cis side of the Golgi
        
        Furthermore, Proteins that have a sequence of AA of KDEL are also sent back to the RER.
        
        COP-II
        
        this COP is responsible for directing the vesicles from the RER to the Golgi
        
        Protein (vesicle) sorting
        
        coated vesicles
        
        functions
        
        favours the bending of the membrane during the formation of the vesicle
        
        allows the selection of the components that have to be inserted and transported into the vesicle
        
        direction and destination
        
        carry proteins
        
        how they leave the Golgi
        
        constitutive secretion
        
        4 more items...
        
        regulated secretion
        
        4 more items...
        
        trafficking
        
        endocytosis
        
        1 more item...
        
        exocytosis
        
        gemmation
        
        Clathrin
        
        from Golgi to plasma membrane or endosomes
        
        Transmembrane protein v-SNARE specifically recognised by the sequences t-SNARE on the target membrane
        
        6-phosphate mannose delivered to lysosomes
  - - - types
        
        cis
        
        medial
        
        trans