The effects of Ca2+ binding on the conformation of calbindin D28K: A nuclear magnetic resonance and microelectrospray mass spectrometry study

Venters, Ronald A.; Benson, Linda M.; Craig, Theodore A.; Paul, Keriann H.; Kordys, David R.; Thompson, Richele J.; Naylor, Stephen; Kumar, Rajiv; Cavanagh, John

doi:10.1016/s0003-2697(03)00084-8

Cited by 23 publications

(23 citation statements)

References 22 publications

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“…A detailed NMR analysis of CB structure (Kojetin et al, 2006), completing earlier work (Klaus et al, 1999; Berggård et al, 2000, 2002a,b; Venters et al, 2003; Venyaminov et al, 2004; Vanbelle et al, 2005), confirmed that upon Ca 2+ binding CB adopts discrete hydrophobic states but also has exposed hydrophobic surfaces in its apo-form. In addition, the regions mediating the interactions with RanBPM, IMPase, Caspase-3 and also its pro-domain were mapped.…”

Section: Buffer or Sensor?supporting

confidence: 56%

Three functional facets of calbindin D-28k

Schmidt¹

2012

Front. Mol. Neurosci.

100

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Many neurons of the vertebrate central nervous system (CNS) express the Ca2+ binding protein calbindin D-28k (CB), including important projection neurons like cerebellar Purkinje cells but also neocortical interneurons. CB has moderate cytoplasmic mobility and comprises at least four EF-hands that function in Ca2+ binding with rapid to intermediate kinetics and affinity. Classically it was viewed as a pure Ca2+ buffer important for neuronal survival. This view was extended by showing that CB is a critical determinant in the control of synaptic Ca2+ dynamics, presumably with strong impact on plasticity and information processing. Already 30 years ago, in vitro studies suggested that CB could have an additional Ca2+ sensor function, like its prominent acquaintance calmodulin (CaM). More recent work substantiated this hypothesis, revealing direct CB interactions with several target proteins. Different from a classical sensor, however, CB appears to interact with its targets both, in its Ca2+-loaded and Ca2+-free forms. Finally, CB has been shown to be involved in buffered transport of Ca2+, in neurons but also in kidney. Thus, CB serves a threefold function as buffer, transporter and likely as a non-canonical sensor.

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Section: Buffer or Sensor?supporting

confidence: 56%

Three functional facets of calbindin D-28k

Schmidt¹

2012

Front. Mol. Neurosci.

100

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“…It should therefore be noted that CB could also have an additional role as a Ca 2+ sensor, as was proposed previously (Berggård et al . 2002b; Venters et al . 2003).…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, CB undergoes Ca 2+ ‐dependent conformational changes, has a many‐fold selectivity for Ca 2+ over Mg 2+ , and its Ca 2+ dissociation constant falls within the physiological range of intracellular free Ca 2+ concentrations (Berggård et al . 2002b; Venters et al . 2003).…”

Section: Discussionmentioning

confidence: 99%

Dual role of calbindin‐D_28K in vesicular catecholamine release from mouse chromaffin cells

Westerink

Rook

Beekwilder

et al. 2006

Journal of Neurochemistry

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Calbindin-D 28K is suggested to play a postsynaptic role in neurotransmission and in the regulation of the intracellular Ca 2+ concentration. However, it is still unclear whether calbindin-D 28K has a role in the regulation of exocytosis, either as Ca 2+ buffer or as Ca 2+ sensor. Amperometric recordings of catecholamine exocytosis from wild-type and calbindin-D 28K knockout mouse chromaffin cells reveal a strong reduction in the number of released vesicles, as well as in the amount of neurotransmitter released per fusion event in knockout cells. However, Ca 2+ current recordings and Ca 2+ imaging experiments, including video-rate confocal laser scanning microscopy, revealed that the intracellular Ca 2+ dynamics are remarkably similar in wild-type and knockout cells. The combined results demonstrate that calbindin-D 28K plays an important and dual role in exocytosis, affecting both release frequency and quantal size, apparently without strong effects on intracellular Ca 2+ dynamics. Consequently, the possibility that calbindin-D 28K functions not only as a Ca 2+ buffer but also as a modulator of vesicular catecholamine release is discussed.

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“…In the mouse kidney, both forms are present and are regulated by vitamin D. In other species, only calbindin-D 28K is expressed in the kidney. Both proteins undergo conformational change upon binding to calcium [254, 256, 265]. We recently solved the structure of Ca 2+ -loaded calbindin-D 28K using NMR spectroscopy [266].…”

Section: Distribution and Regulation Of Vitamin D-dependent Proteimentioning

confidence: 99%

Vitamin D and the kidney

Kumar¹,

Tebben²,

Thompson³

2012

Archives of Biochemistry and Biophysics

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The effects of Ca2+ binding on the conformation of calbindin D28K: A nuclear magnetic resonance and microelectrospray mass spectrometry study

Cited by 23 publications

References 22 publications

Three functional facets of calbindin D-28k

Three functional facets of calbindin D-28k

Dual role of calbindin‐D_28K in vesicular catecholamine release from mouse chromaffin cells

Vitamin D and the kidney

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The effects of Ca2+ binding on the conformation of calbindin D28K: A nuclear magnetic resonance and microelectrospray mass spectrometry study

Cited by 23 publications

References 22 publications

Three functional facets of calbindin D-28k

Three functional facets of calbindin D-28k

Dual role of calbindin‐D28K in vesicular catecholamine release from mouse chromaffin cells

Vitamin D and the kidney

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Product

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Dual role of calbindin‐D_28K in vesicular catecholamine release from mouse chromaffin cells