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A
20kDa protein abundant in brain and testes (Aderem,
1992; Blackshear, 1993).
Unlike MARKS, MRP neither bundles microfilaments nor alters the kinetics
of actin polymerization (Wohnsland
et al, 2000). An
interaction between MacMARKS and dynamitin (a subunit of the dynactin complex),
has been detected in vitro (Yue
et al, 2000)
and in vivo (Jin
et al, 2001)
References:-
Aderem, A. (1992).
"The MARKS brothers: A family of protein kinase C substrates." Cell
71, 713-716.
Blackshear, P.J.
(2000). "The MARKS family of cellular protein kinase C substrates." J.Biol.Chem.
268, 1501-1504.
Jin, T., Yue, L. & Li, J. (2001) In
vivo interaction between dynamitin and MacMARKS detected by the fluorescence
resonance energy transfer method., J.Biol.Chem. 276, 12879-12884.
Wohnsland,
F., Steinmetz, M. O., Aebi, U. & Vergeres, G. (2000). “MARCKS-related
protein binds to actin without significantly affecting actin polymerization of
network structure.” J.Struct.Biol. 131, 217-224.
Yue, L., Lu, S., Garces, J., Jin, T. & Li,
J. (2000) Protein kinase C-regulated dynamitin-macrophage-enriched myristoylated
alanin-rich C kinase substrate interaction is involved in macrophage cell
spreading., J.Biol.Chem. 276, 23948-23956.
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