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Related Experiment Videos

Cell type differences in Golgi retention signals for transmembrane proteins

B L Tang1, S H Low, S H Wong

  • 1Institute of Molecular and Cell Biology, National University of Singapore.

European Journal of Cell Biology
|April 1, 1995
PubMed
Summary

The transmembrane domain of Golgi proteins can signal for retention, but this signal is interpreted differently by various cell types. Proteins lacking flanking sequences may bypass the Golgi and go to lysosomes.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • The transmembrane domain (TMD) of certain Golgi-resident proteins contains signals for retention within the Golgi apparatus.
  • Beta-galactoside alpha 2,6-sialyltransferase (ST) and N-acetylglucosaminyltransferase 1 (NT) are examples of such proteins.

Purpose of the Study:

  • To investigate the role of the TMD in Golgi retention of ST and NT.
  • To determine how cell type influences the interpretation of Golgi retention signals.
  • To identify the destination of chimeric proteins that escape Golgi retention.

Main Methods:

  • Construction of chimeric proteins using the TMD of ST and NT with dipeptidyl peptidase IV.
  • Expression and analysis in MDCK, COS, and CHO cells using indirect immunofluorescence microscopy.

Related Experiment Videos

  • Pulse-chase experiments and biochemical analysis with endoglycosidase H.
  • Colocalization studies with Golgi and lysosomal markers.
  • Monitoring cell surface appearance of chimeric proteins.

    • Main Results:

    • Chimeric proteins were retained in the Golgi in MDCK and COS cells but transported to post-Golgi vesicular structures in CHO cells.
    • These vesicular structures in CHO cells did not colocalize with Golgi markers but did colocalize with lysosomal markers.
    • Biochemical analysis indicated transport beyond the medial Golgi, and proteins were eventually delivered to the lysosomal compartment.
    • Inclusion of flanking sequences restored or improved Golgi retention.

    Conclusions:

    • Golgi retention signals within TMDs are cell-type dependent.
    • Golgi retention of type II glycosyltransferases requires both the TMD and flanking sequences.
    • Proteins escaping Golgi retention can be directed to the lysosomal pathway.