Rockefeller University Press

Table I

Effect of Mutations in the HA TM on Kinetics of Transport through the Secretory Pathway

Protein	Percent in Golgi after 30 min	Percent at surface after 60 min	Percent at surface after 180 min
HA	73	48	87
4A507	42	47	71
4A511	70	32	47
2A511	61	57	89
2A514	5	10	7
2A517	44	61	80
4A520	64	53	70
2A520	61	47	70
4A524	37	45	87
4A528	54	84	90
5A531	45	84	97
A516S	42	77	97
G520S	68	72	97
S521A	68	71	96
ΔG520ΔS521	65	53	73

Protein	Percent in Golgi after 30 min	Percent at surface after 60 min	Percent at surface after 180 min
HA	73	48	87
4A507	42	47	71
4A511	70	32	47
2A511	61	57	89
2A514	5	10	7
2A517	44	61	80
4A520	64	53	70
2A520	61	47	70
4A524	37	45	87
4A528	54	84	90
5A531	45	84	97
A516S	42	77	97
G520S	68	72	97
S521A	68	71	96
ΔG520ΔS521	65	53	73

Results are shown from a representative pulse-chase experiment on MDCK cells permanently expressing various HA mutants. Arrival at the Golgi was monitored by the appearance of terminally glycosylated HA, which migrates more slowly during PAGE. Arrival at the cell surface was measured as the percentage of HA that was converted into its HA1 and HA2 subunits by trypsin added to the chase medium. An exception was the 4A511 mutant, which was degraded by trypsin. Arrival of this protein to the cell surface was measured by biotinylation.

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