During the last twenty years,
we have been responsible for the introduction and development
of caged compounds for biophysical and physiological
studies. These are novel photolabile compounds which
on u-v illumination release the caged substrate (ATP,
ADP, Pi, Ca2+, Mg2+, etc.) in the msec-microsec time
range and thus synchronously and rapidly initiate biological
processes. We plan to continue to develop this strategy
to provide novel photorelease techniques for cellular
and molecular studies.
C. Selected Relevant Publications
Ellis-Davies, G.C.R. and Kaplan, J.H. (1988) A new
class of photolabile chelators for the rapid release
of divalent cations: the synthesis of caged Ca and caged
Mg. J. Organic. Chem.,153:1966-1969.
Ellis-Davies, G.C.R. and Kaplan, J.H. (1990) Binding
of Na+ ions to the Na+,K+-ATPase increases the reactivity
of an essential residue in the ATP binding domain. J.
Biol. Chem., 265:20570-20576.
Argüello J. and Kaplan, J.H. (1991) Evidence for
essential carboxyls in the cation binding domain of
the Na,K-ATPase. J. Biol. Chem., 266:14627-14635.
McCray, J.A., Ellis-Davies, G.C.R., Fidler-Lin, N.
and Kaplan, J.H. (1992) Rate of release of Ca2+ following
laser photolysis of the DM-nitrophen-Ca2+ complex, Biochemistry,
31:8856-8861.
Lutsenko, S., and Kaplan, J.H. (1992) Evidence of a
role for the Na,K-ATPase ?-subunit in active cation
transport. Ann. NY Acad. Sci., 671:147-155.
Ellis-Davies, G.C.R. and Kaplan, J.H. (1993) Modification
of lysine-501 in the Na,K-ATPase reveals coupling between
cation occupancy and changes in the ATP binding domain.
J. Biol. Chem.,268:11622-11627.
Lutsenko, S. and Kaplan, J.H. (1993) An essential role
of the extra-cellular domain of the Na,K-ATPase ?-subunit
in ion-occlusion. Biochemistry, 32:6737-6743.
Argüello, J. and Kaplan, J.H. (1994) Glu779, an
intramembrane carboxyl is essential for monovalent cation
binding by the Na,K-ATPase. J. Biol. Chem., 269:6892-6899.
Petrukhin, K., Lutsenko, S., Chernov, I., Ross, B.M.,
Kaplan, J.H. and Gilliam, T.C. Characterization of the
Wilson disease gene encoding a P-type copper transporting
ATPase: genomic organization, alternative splicing,
and structure/function predictions. Human Molecular
Genetics, 3:1647-1656, 1994
Ellis-Davies, G.C.R. and Kaplan, J.H. (1994) Nitrophenyl-EGTA,
a photolabile chelator that selectively binds Ca2+ with
high affinity and releases it rapidly on photolysis.
Proc. Natl. Acad. Sci., USA, 91:187-191.
Lutsenko, S. and Kaplan, J.H. (1994) Molecular events
in close proximity to the membrane upon ligand-binding
by Na,K-ATPase. J. Biol. Chem., 269:4555-4564.
Shin, J.M., Kajimura, M., Argüello, J.A., Kaplan,
J.H. and Sachs, G. (1994) Biochemical Identification
of transmembrane segments of the Ca2+-ATPase of sarcoplasmic
reticulum. J. Biol. Chem., 269:22533-37.
Valdivia, H.H., Kaplan, J.H., Ellis-Davies, G.C.R.
and Lederer, W.J. (1995) Rapid adaptation of cardiac
ryanodine receptors: Modulation by Mg2+ and phosphorylation.
Science, 267: 1997-2000.
Lutsenko, S., Anderko, R. and Kaplan, J.H. (1995) Membrane
disposition of the M5-M6 hairpin of Na,K-ATPase a-subunit
is ligand dependent. Proc. Nat. Acad. Sci. USA, 92:
7936-7940.
Ellis-Davies, G.C.R., Kaplan, J.H. and Barsotti, R.J.
(1996) Laser photolysis of caged calcium: Rates of calcium
release by nitrophenyl-EGTA and DM-nitrophen. Biophys.
J., 70: 1006-1016.
Lutsenko, S., Daoud, S. and Kaplan, J.H. (1997) Identification
of two conformationally-sensitive cys residues at the
extracellular surface of the Na,K-ATPase a-subunit.
J. Biol. Chem., 272: 5249-5255.
Lutsenko, S., Petrukhin, K., Cooper, M.J., Gilliam,
C.T. and Kaplan, J.H. (1997) N-terminal domains of human
copper-transporting adenosine triphosphatases (the Wilson’s
and Menkes disease proteins) bind copper selectivity
in vivo and in vitro with stoichiometry of one copper
per metal-binding repeat. J. Biol. Chem., 272:18939-18944.
Lutsenko, S., Petrukhin, K., Gillian, T.C. and Kaplan,
J.H. (1997) Heterologous expression of the metal-binding
domain of human copper-transporting ATPases (P1 ATPases).
Ann. NY Acad. Sci., 834: 155-157.
Gatto, C., Wang, A.X. and Kaplan, J.H. (1998) The M4M5
cytoplasmic loop of the Na,K-ATPase, overexpressed in
E. coli, binds nucleoside triphosphates with the same
selectivity as the intact native protein. J. Biol. Chem.,
10578-10585.
Gatto, C. Thornewell, S.J., Holden, J.P. and Kaplan,
J.H. (1999) Cys-577 is a conformationally mobile residue
in the ATP-binding domain of the Na,K-ATPase a-subunit.
J. Biol. Chem., 274: 24995-25003.
Gatto, C., Lutsenko, S., Shin, J., Saks, G. and Kaplan,
J.H. (1999) Stabilization of the H,K-ATPase M5M6 membrane
hairpin by K+ ions: Mechanistic significance for P2-type
ATPases. J. Biol. Chem., Communication, 274: 13737-13740.
Hu, Y-K. and Kaplan, J.H. (2000) Site-directed labelling
of extracellular loops in a membrane protein: The toplogy
of the Na,K-ATPase a-subunit. J. Biol. Chem., 275:19185-19191.
Eisses, J.F., Stasser, J.P., Ralle, M., Kaplan, J.H.
and Blackburn, N.J. (2000) Domain I and III of LCCS
interest via a cysteine-bridged dicopper (I) cluster.
Biochemistry, 39: 7337-7342.
Hu, Y-K., Gatto, C., Eisses, J.D. and Kaplan, J.H.
(2000) Expression of active cysteine-less forms of the
Na,K-ATPase a-subunit in baculovirus-infected insect
cells. J. Biol. Chem., 275: 30734-30739.
Gatto, C., McCloud, S. and Kaplan, J.H. (2001) Heterologous
expression of Na,K-ATPase in insect cells:Intracellulardistribution
of pump subunits. Am. J. Physiol. Cell Physiol. 281:C982-C992.
Tsivkoskii, R., Eisses, J.F., Kaplan, J.H. and Lutsenko,
S. (2002) Functional properties of the copper-transporting
ATPase ATP7 (The Wilson's Disease Protein) expressed
in insect cells. J. Biol. Chem., 277:976-983.
Eisses, J.D. and Kaplan, J.H. (2002) Molecular characterization
of hCTR1, the human copper uptake protein. J. Biol.
Chem., 277:29162-29171.
Geibel, S., Kaplan, J.H., Bamberg, E. and Friedrich,
T. (2003) Conformational dynamics of the Na,K-ATPase
probed by voltage clamp fluorometry. Proc. Natl. Acad.
Sci., USA, 100:964-969.
Costa, C.J., Gatto, C. and Kaplan, J.H. (2003) Interactions
between Na,K-ATPase a-subunit ATP-binding domains. J.
Biol. Chem., 278:9176-9184.
Laughery , MD, McLoud S, and Kaplan JH. (2003) Mutational
analysis of the interactions of the alpha and beta subunits
of the Na,K-ATPase. Ann N Y Acad Sci., 986:273-4
Laughery, MD, Todd, and Kaplan JH (2003) Mutational
analysis of alpha -beta subunit interactions in the
delivery of Na,K-ATPase heterodimers to the plasma membrane.
J Biol Chem. 278, 34794-34803.
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