Capacitation dependent activation of tyrosine phosphorylation generates two sperm head plasma membrane proteins with high primary binding affinity for the zona pellucida

2001 ◽  
Vol 60 (1) ◽  
pp. 107-115 ◽  
Author(s):  
F.M. Flesch ◽  
E. Wijnand ◽  
C.H.A. van de Lest ◽  
B. Colenbrander ◽  
L.M.G. van Golde ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Tyrosine Phosphorylation ◽  
Binding Affinity ◽  
Zona Pellucida ◽  
Sperm Head ◽  
Plasma Membrane Proteins

Further characterization of boar sperm plasma membrane proteins with affinity for the porcine zona pellucida

1985 ◽  
Vol 12 (1) ◽  
pp. 91-100 ◽  
Author(s):  
R. N. Peterson ◽  
L. Henry ◽  
W. Hunt ◽  
N. Saxena ◽  
L. D. Russell
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Zona Pellucida ◽  
Plasma Membrane Proteins ◽  
Boar Sperm ◽  
Sperm Plasma Membrane

Detergent fractionation with subsequent subtractive suppression hybridization as a tool for identifying genes coding for plasma membrane proteins

2009 ◽  
Vol 18 (6) ◽  
pp. 527-535 ◽  
Author(s):  
Andreas Lange ◽  
Claudia Kistler ◽  
Tanja B. Jutzi ◽  
Alexandr V. Bazhin ◽  
Claus Detlev Klemke ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Plasma Membrane Proteins ◽  
Subtractive Suppression Hybridization

scholarly journals pH-dependent Cargo Sorting from the Golgi

2011 ◽  
Vol 286 (12) ◽  
pp. 10058-10065 ◽  
Author(s):  
Chunjuan Huang ◽  
Amy Chang
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Atpase Activity ◽  
Secretory Pathway ◽  
Ph Dependence ◽  
Glucose Deprivation ◽  
Ph Homeostasis ◽  
Plasma Membrane Proteins ◽  
Cytosolic Ph ◽  
Cargo Sorting

The vacuolar proton-translocating ATPase (V-ATPase) plays a major role in organelle acidification and works together with other ion transporters to maintain pH homeostasis in eukaryotic cells. We analyzed a requirement for V-ATPase activity in protein trafficking in the yeast secretory pathway. Deficiency of V-ATPase activity caused by subunit deletion or glucose deprivation results in missorting of newly synthesized plasma membrane proteins Pma1 and Can1 directly from the Golgi to the vacuole. Vacuolar mislocalization of Pma1 is dependent on Gga adaptors although no Pma1 ubiquitination was detected. Proper cell surface targeting of Pma1 was rescued in V-ATPase-deficient cells by increasing the pH of the medium, suggesting that missorting is the result of aberrant cytosolic pH. In addition to mislocalization of the plasma membrane proteins, Golgi membrane proteins Kex2 and Vrg4 are also missorted to the vacuole upon loss of V-ATPase activity. Because the missorted cargos have distinct trafficking routes, we suggest a pH dependence for multiple cargo sorting events at the Golgi.

scholarly journals 5-Iodonaphthyl-1-azide labeling of plasma membrane proteins adjacent to specific sites via energy transfer

1997 ◽  
Vol 1324 (2) ◽  
pp. 320-332 ◽  
Author(s):  
Bruce I Meiklejohn ◽  
Noorulhuda A Rahman ◽  
Deborah A Roess ◽  
B.George Barisas
Keyword(s):  
Plasma Membrane ◽  
Energy Transfer ◽  
Membrane Proteins ◽  
Plasma Membrane Proteins

scholarly journals Characterization of Plasma Membrane Proteins in Mammalian Kidney

1969 ◽  
Vol 244 (13) ◽  
pp. 3561-3569
Author(s):  
D F Fitzpatrick ◽  
G R Davenport ◽  
L Forte ◽  
E J Landon
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Plasma Membrane Proteins ◽  
Mammalian Kidney
Sign in / Sign up

Export Citation Format

Share Document