(Sibling family proteins) that have extended domains termed “intrinsically disordered” and can adopt different conformations when interacting with different
“targets”, such as crystal surfaces. Such proteins have been shown to participate
in polymorph selection (aragonite/calcite) in mollusks (Evans 2008; McMahon
et al. 2005; Metzler et al. 2010). In addition to IDP domains, domains with dense
clusters of negative charge, such as phosphates found in phosphophoryn of dentin,
could conceivably play similar roles in different biomineralizing systems. Perhaps
we should look for analogous function of certain domains, rather than specific
proteins, as a common thread in biomineralization.
There has been a radical shift in the kinds of models considered to explain the
formation of biominerals. Just a few decades ago, it would have been difficult to
foresee amorphous precursors and proteins with domains of poorly defined conformation playing roles in biomineralization, but these are now well established. There
are exciting developments before us. Current research is so robust that we can
foresee considerable progress in the near future.
Acknowledgments The authors gratefully acknowledge support for research in their respective
laboratories from DOE grant DE-FG02-07ER15899, NSF grant DMR&CHE-0613972, and
UW-Madison Hamel Award to PUPAG, and NSF grant 0444724 and Committee on Research of
UC Berkeley to FW.
References
Aizenberg J, Hanson J, Koetzle TF, Weiner S, Addadi L (1997) Control of macromolecule
distribution within synthetic and biogenic single calcite crystals. J Am Chem Soc 119:881–886
Aizenberg J, Muller DA, Grazul JL, Hamann DR (2003) Direct fabrication of large micropatterned
single crystals. Science 299:1205–1208
Alvares K, Dixit SE, Lux E, Veis A (2009) Echinoderm phosphorylated matrix proteins UTMP16
and UTMP19 have different functions in sea urchin tooth mineralization. J Biol Chem
284:26149–26160
Ameye L, Hermann R, Wilt F, Dubois P (1999) Ultrastructural localization of proteins involved in
sea urchin biomineralization. J Histochem Cytochem 47:1189–1200
Ameye L, Becker G, Killian C, Wilt F, Kemps R, Kuypers S, DuBois P (2001) Proteins and
saccharides of the sea urchin organic matrix of mineralization: characterization and localization in the spine skeleton. J Struct Biol 134:56–66
Banfield JF, Welch SA, Zhang HZ, Ebert TT, Penn RL (2000) Aggregation-based crystal growth
and microstructure development in natural iron oxyhydroxide biomineralization products.
Science 289:751–754
Beniash E, Aizenberg J, Addadi L, Weiner S (1997) Amorphous calcium carbonate transforms into
calcite during sea urchin larval spicule growth. Proc R Soc Lond Biol 264:461–465
Beniash E, Addadi L, Weiner S (1999) Cellular control over spicule formation in sea urchin
embryos: a structural approach. J Struct Biol 125:50–62
Beniash E, Metzler R, Lam RSK, Gilbert PUPA (2009) Transient amorphous calcium phosphate in
forming enamel. J Struct Biol 166:133–143
Benson S, Jones EME, Benson N, Wilt F (1983) Morphology of the organic matrix of the spicule
of the sea urchin larva. Exp Cell Res 148:249–253
7 Molecular Aspects of Biomineralization of the Echinoderm Endoskeleton
219
“targets”, such as crystal surfaces. Such proteins have been shown to participate
in polymorph selection (aragonite/calcite) in mollusks (Evans 2008; McMahon
et al. 2005; Metzler et al. 2010). In addition to IDP domains, domains with dense
clusters of negative charge, such as phosphates found in phosphophoryn of dentin,
could conceivably play similar roles in different biomineralizing systems. Perhaps
we should look for analogous function of certain domains, rather than specific
proteins, as a common thread in biomineralization.
There has been a radical shift in the kinds of models considered to explain the
formation of biominerals. Just a few decades ago, it would have been difficult to
foresee amorphous precursors and proteins with domains of poorly defined conformation playing roles in biomineralization, but these are now well established. There
are exciting developments before us. Current research is so robust that we can
foresee considerable progress in the near future.
Acknowledgments The authors gratefully acknowledge support for research in their respective
laboratories from DOE grant DE-FG02-07ER15899, NSF grant DMR&CHE-0613972, and
UW-Madison Hamel Award to PUPAG, and NSF grant 0444724 and Committee on Research of
UC Berkeley to FW.
References
Aizenberg J, Hanson J, Koetzle TF, Weiner S, Addadi L (1997) Control of macromolecule
distribution within synthetic and biogenic single calcite crystals. J Am Chem Soc 119:881–886
Aizenberg J, Muller DA, Grazul JL, Hamann DR (2003) Direct fabrication of large micropatterned
single crystals. Science 299:1205–1208
Alvares K, Dixit SE, Lux E, Veis A (2009) Echinoderm phosphorylated matrix proteins UTMP16
and UTMP19 have different functions in sea urchin tooth mineralization. J Biol Chem
284:26149–26160
Ameye L, Hermann R, Wilt F, Dubois P (1999) Ultrastructural localization of proteins involved in
sea urchin biomineralization. J Histochem Cytochem 47:1189–1200
Ameye L, Becker G, Killian C, Wilt F, Kemps R, Kuypers S, DuBois P (2001) Proteins and
saccharides of the sea urchin organic matrix of mineralization: characterization and localization in the spine skeleton. J Struct Biol 134:56–66
Banfield JF, Welch SA, Zhang HZ, Ebert TT, Penn RL (2000) Aggregation-based crystal growth
and microstructure development in natural iron oxyhydroxide biomineralization products.
Science 289:751–754
Beniash E, Aizenberg J, Addadi L, Weiner S (1997) Amorphous calcium carbonate transforms into
calcite during sea urchin larval spicule growth. Proc R Soc Lond Biol 264:461–465
Beniash E, Addadi L, Weiner S (1999) Cellular control over spicule formation in sea urchin
embryos: a structural approach. J Struct Biol 125:50–62
Beniash E, Metzler R, Lam RSK, Gilbert PUPA (2009) Transient amorphous calcium phosphate in
forming enamel. J Struct Biol 166:133–143
Benson S, Jones EME, Benson N, Wilt F (1983) Morphology of the organic matrix of the spicule
of the sea urchin larva. Exp Cell Res 148:249–253
7 Molecular Aspects of Biomineralization of the Echinoderm Endoskeleton
219