Mitochondrial Morphogenesis, Dendrite Development,
and Synapse Formation in Cerebellum Require both
Bcl-w and the Glutamate Receptor d2
Qiong A. Liu1*, Helen Shio2
1Medical Department, Brookhaven National Laboratory, Upton, New York, United States of America, 2Bio-Imaging Resource Center, Rockefeller University, New York,
New York, United States of America
Bcl-w belongs to the prosurvival group of the Bcl-2 family, while the glutamate receptor d2 (Grid2) is an excitatory receptor
that is specifically expressed in Purkinje cells, and required for Purkinje cell synapse formation. A recently published result as
well as our own findings have shown that Bcl-w can physically interact with an autophagy protein, Beclin1, which in turn has
been shown previously to form a protein complex with the intracellular domain of Grid2 and an adaptor protein, nPIST. This
suggests that Bcl-w and Grid2 might interact genetically to regulate mitochondria, autophagy, and neuronal function. In this
study, we investigated this genetic interaction of Bcl-w and Grid2 through analysis of single and double mutant mice of
these two proteins using a combination of histological and behavior tests. It was found that Bcl-w does not control the cell
number in mouse brain, but promotes what is likely to be the mitochondrial fission in Purkinje cell dendrites, and is required
for synapse formation and motor learning in cerebellum, and that Grid2 has similar phenotypes. Mice carrying the double
mutations of these two genes had synergistic effects including extremely long mitochondria in Purkinje cell dendrites, and
strongly aberrant Purkinje cell dendrites, spines, and synapses, and severely ataxic behavior. Bcl-w and Grid2 mutations
were not found to influence the basal autophagy that is required for Purkinje cell survival, thus resulting in these
phenotypes. Our results demonstrate that Bcl-w and Grid2 are two critical proteins acting in distinct pathways to regulate
mitochondrial morphogenesis and control Purkinje cell dendrite development and synapse formation. We propose that the
mitochondrial fission occurring during neuronal growth might be critically important for dendrite development and
synapse formation, and that it can be regulated coordinately by multiple pathways including Bcl-2 and glutamate receptor
Citation: Liu QA, Shio H (2008) Mitochondrial Morphogenesis, Dendrite Development, and Synapse Formation in Cerebellum Require both Bcl-w and the
Glutamate Receptor d2. PLoS Genet 4(6): e1000097. doi:10.1371/journal.pgen.1000097
Editor: Harry Orr, University of Minnesota, United States of America
Received February 6, 2008; Accepted May 13, 2008; Published June 13, 2008
Copyright: ? 2008 Liu, Shio. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted
use, distribution, and reproduction in any medium, provided the original author and source are credited.
Funding: Dr. Qiong A. Liu and this work has been mostly supported by a Rockefeller University fund to Dr. Nathaniel Heintz’s lab at Rockefeller University and the
Brookhaven National Laboratory directorate fund to Dr. Qiong A. Liu.
Competing Interests: The authors have declared that no competing interests exist.
* E-mail: email@example.com
Mitochondria have been shown to undergo morphological
changes in many neurodegenerative and psychiatric diseases,
suggesting their vital role in maintaining the normal function of
neuron cells. One of the morphological changes in mitochondria is
the length or size, which can be controlled by mitochondrial
growth or mitochondrial fission/fusion cycles. Mitochondria are
dynamic organelles that can undergo fission, fusion, branching,
and change in subcellular distribution [1–3], resulting in the
exchange of their genetic materials, alteration of their shape, and
increase or decrease of their number [1–3]. This dynamic nature
of mitochondria is also critically important for energy generation,
calcium buffering, and control of apoptosis. Mitochondrial fission
and fusion is normally a well-balanced event; when the fission is
blocked, the length of mitochondria increases due to ongoing
fusion, and mitochondrial fission sites persist as constriction sites
due to the slowdown of fission, whiles when the fusion is inhibited,
mitochondria usually appear fragmented . Mitochondrial
number increases during cellular division, growth, and differen-
tiation via the fission process . However, excessive fission can
stimulate apoptosis , and cause neurodegenerative diseases .
In cultured healthy neurons, mitochondrial fission and fusion
proteins have been shown to regulate the morphology and
plasticity of dendritic spines and synapses . In addition,
glutamate  and synaptic activity  modulates the motility
and fusion/fission balance of mitochondria and controls mito-
chondrial distribution in dendrites . Several proteins have been
identified in a variety of species to mediate mitochondrial fission or
fusion process [2,3], however, little is known about the signaling
molecules that activate these processes.
Cerebellar Purkinje cells are characterized by large and highly
branched dendritic arbors in the brain. Over 90% of Purkinje cell
dendritic spines form excitatory synapses with granule cell parallel
fiber axons, which relay information from pre-cerebellar nuclei to
Purkinje cells. Grid2 is strongly expressed in Purkinje cells , and
localizes specifically to Purkinje cell/ parallel fiber synapses
[10,11]. Analysis of Grid2 knockout mice , and Hotfoot mice
carrying spontaneous loss-of-function mutations in Grid2 [13,14]
has demonstrated that these mice exhibit an impaired function on
motor coordination and learning tasks, and have structural and
functional defects in Purkinje cell/granule cell parallel fiber
PLoS Genetics | www.plosgenetics.org1June 2008 | Volume 4 | Issue 6 | e1000097
synapses and altered long term depression [12,15,16]. Physiologic
studies of Grid2Lc, the Lurcher dominant mutation have
established that the Grid2Lcmutation results in inward Ca2+/
Na+current and constitutive activation of the d2 glutamate
receptor, and also that the Grid2Lcreceptor has similar channel
properties to both NMDA  and AMPA receptors [18,19].
Activation of Grid2Lcalso induces autophagy and degeneration of
Purkinje cells. This degeneration might be mediated through
interaction of Grid2 with its downstream autophagy protein,
Beclin1 . Autophagy is a conserved mechanism for degrada-
tion of proteins and other subcellular constituents, and is often
involved in cell and tissue remodeling or cell death . Two
recent reports demonstrated that Purkinje cells also degenerate
without the presence of the basal level of autophagy [22,23].
Bcl-2 family members have been most extensively studied in the
context of apoptotic cell death . The Bcl-2 family was divided
into the pro-survival members that protect cells from being killed,
and the pro-death members that kill cells. Bcl-w belongs to the
pro-survival group of the Bcl-2 family that includes Bcl-2, Bcl-XL,
A1, and CED-9 [25,26]. These proteins function to protect cells
from apoptosis by binding to the outer membrane of mitochondria
through their C-terminal hydrophobic domain, thereby prevent-
ing the release of several apoptosis proteins from mitochondria
into the cytoplasm. They include the caspase regulatory proteins
and proteins that lead to DNA fragmentation and chromosome
condensation . Bcl-w is widely expressed in a variety of tissues,
but predominantly in adult brain and spinal cord . The
expression of Bcl-w in brain increases during the postnatal
development and is maintained at high levels in the adult brain
including cerebellum Purkinje cells, where it is localized to
Purkinje cell soma  and dendrites (Lab Vision Corporation),
whereas Bcl-XL, the only other pro-survival member that is
expressed in adult brain had much lower level of expression .
Bcl-w2/2mice are smaller during the early postnatal development,
but viable and normal in appearance as adults. Both apoptotic and
non-apoptotic cell death have been observed in the testes of Bcl-
A recent report as well as our own findings demonstrated that
several other survival members of the Bcl-2 family including Bcl-w
could also bind to the autophagy protein, Beclin1 [32–34]. Beclin1
has been shown previously to form a protein complex with an
adaptor protein, nPIST, and the intracellular domain of Grid2
. Thus, Bcl-w might interact genetically with Grid2 to regulate
mitochondrial, autophagy, and neuronal function.
In this study, we aim to understand how Bcl-w and Grid2
interact genetically to regulate mitochondria, autophagy, and
neuronal function using Bcl-w and Grid2 null mutant mice. We
show that the survival member of the Bcl-2 family member, Bcl-w
does not control the cell number in brain, but promotes what is
likely to be the mitochondrial fission in Purkinje cell dendrites, and
is required for the Purkinje cells/parallel fibers synapses and motor
learning. We demonstrated that the excitatory receptor Grid2
could regulate mitochondrial length, and the mutation of this
protein shares the similar phenotypes in cerebella with the loss-of-
function of Bcl-w. Comparative analyses of single and double
mutant mice of Bcl-w and Grid2 further indicate that these
molecules act synergistically to regulate mitochondrial length and
to control the development of Purkinje cell dendrites, dendritic
spines, and synapse formation. We further show that no evidence
of alteration of autophagy in single and double mutant mice was
observed, and the potential upregulation of Beclin1 in Bcl-w2/2
mice and overexpression of Beclin1 was not sufficient to activate
autophagy. We have thus identified Bcl-w and Grid2 as two
critical proteins acting in distinct pathways to control mitochon-
drial morphogenesis and Purkinje cell development in the mouse
Bcl-w and Grid2 Activity Regulate Mitochondrial Length
in Purkinje Cell Dendrites
Since Bcl-w binds to Beclin1, which in turn can form a protein
complex with nPIST and the intracellular domain of Grid2 ,
the possibility arises that Bcl-w may function downstream of
Grid2. We thus examined if Bcl-w2/2[30,31] and Grid2ho24J(2/2)
mice [14,35,36] that carry spontaneous null mutation of the Grid2
gene share similar phenotypes. Since Bcl-w binds to the outer
membrane of mitochondria to regulate apoptotic activity , we
examined both cell numbers (see below) and the morphology of
mitochondria in Bcl-w2/2and Grid2ho24J(2/2)mice by electron
microscopy (EM). Purkinje cells were focused on because Grid2 is
only expressed in Purkinje cells [9–11], and Bcl-w also had strong
expression in these cells in adult brain [28,29].
In these EM micrograph, profiles of mitochondria collected from
longitudinal sections of dendritic tracks in electron micrographs
mice (Figure 1A). The lengths of mitochondria were thus measured
and quantified. Palay and Chan-Palay  have demonstrated
using EM method that the mitochondrial lengths in Purkinje cells of
wild type mice are ,0.1–0.6 m. In the present study, wild type mice
yielded an average value ,0.7 – 0.8 m, with about two third of
mitochondria measuring between 0.1–0.8 m (Figure 1B). This is
similar to the previous electron micrographic estimates . In
Bcl-w2/2mice, the average length of mitochondriawas increased to
,1.4–1.5 m (Figure 1A, B), similarly to that in Grid2ho24J(2/2)mice,
,1.3–1.6 m. Both numbers are significantly different from that
obtained in wild type mice (Figure 1B). In addition, it was notified
upon detailed examination of the micrographs that mitochondria in
both Bcl-w2/2and Grid2ho24J(2/2)mice often contained points
where they became constricted (Figure 1A). This observation
A neuron cell is composed of cell body, axons, and
dendrites. Dendritic spines on dendrites form synapses
with axons of other neurons, establishing communication
between neuron cells. Dendrite development and synapse
formation are therefore important for neuronal function.
Although many genes have been previously identified as
affecting the development of dendrites and synapses, the
apoptosis Bcl-2 family members have not yet been shown
to regulate these processes. In this study, a Bcl-2 family
survival member, Bcl-w, was found not to affect cell death,
but to be required for synapse formation and motor
learning in mouse cerebellum. Bcl-w also appears to
control dendrite development as double null mutant mice
of Bcl-w and the glutamate receptor d2 (Grid2) have severe
defects in Purkinje cell dendrites, spines, and synapses. In
addition, Bcl-w and Grid2 act synergistically to promote
what is likely to be mitochondrial fission in Purkinje cells.
Neither the survival members of the Bcl-2 family nor the
excitatory receptors have been demonstrated previously
to regulate mitochondrial morphogenesis in brain. We
conclude that neuronal dendrite development and syn-
apse formation require perhaps mitochondrial fission that
can be controlled by two critical pathways including Bcl-w
Bcl-w and Grid2 Control Dendrite Development
PLoS Genetics | www.plosgenetics.org2June 2008 | Volume 4 | Issue 6 | e1000097
using MetaVue acquisition software (Universal Imaging), and 20X
water lens, and used to quantify Purkinje cell dendritic branches.
The spines and dendrites were photographed from combined
images from Z-stack (Figure 5A). The spines on dendritic branches
of the first Strahler order (Figure 5B) were photographed using
100X oil lens. The number of mice examined was indicated in
We appreciate the support of Dr. Nathaniel Heintz at Rockefeller
University for this work that were mostly performed in his laboratory,
and his permission for us to publish this paper on our own. We thank Dr.
Grant MacGregor from Emory University (currently at University of
California, Irvine) for providing us the Bcl-w knockout mice, and Jackson
lab for Grid2ho24J(2/2)mice. We are grateful to Bio-Imaging Resource
Center at Rockefeller University for providing the DIC microscope, and to
Greengard lab at Rockefeller University for allowing us to use their handy
Cryosectioner. We also thank Dr. Andrew Gifford for his editorial
comments for this manuscript.
Conceived and designed the experiments: QL. Performed the experiments:
QL HS. Analyzed the data: QL. Contributed reagents/materials/analysis
tools: QL HS. Wrote the paper: QL. Performed electromicroscopy
1. Polyakov VY, Soukhomlinova MY, Fais D (2003) Fusion, fragmentation, and
fission of mitochondria. Biochemistry (Mosc) 68: 838–849.
2. Okamoto K, Shaw JM (2005) Mitochondrial morphology and dynamics in yeast
and multicellular eukaryotes. Annu Rev Genet 39: 503–536.
3. Chan DC (2006) Mitochondrial Fusion and Fission in Mammals. Annu Rev Cell
Dev Biol 22: 79–99.
4. Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002) Molecular
Biology of the Cell (4thedition). GS Garland Science Taylor & Francis group. pp
5. Youle RJ, Karbowski M (2005) Mitochondrial fission in apoptosis. Nat Rev Mol
Cell Biol 6: 657–663.
6. Bossy-Wetzel E, Barsoum M, Godzik A, Schwarzenbacher R, Lipton SA (2003)
Mitochondrial fission in apoptosis, neurodegeneration and aging. Curr Opin
Cell Biol 15: 706–716.
7. Li Z, Okamoto KI, Hayashi Y, Sheng M (2004) The importance of dendritic
mitochondria in the morphogenesis and plasticity of spines and synapses. Cell
8. Rintoul GL, Filiano AJ, Brocard JB, Kress GJ, Reynolds IJ (2003) Glutamate
decreases mitochondrial size and movement in primary forebrain neurons.
J Neurosci 23: 7881–7888.
9. Araki K, Meguro H, Kushiya E, Takayama C, Inoue Y, et al. (1993) Selective
expression of the glutamate receptor channel d2 subunit in cerebellar Purkinje
cells. Biochem Biophys Res Commun 197: 1267–1276.
10. Landsend AS, Amiry-Moghaddam M, Matsubara A, Bergersen L, Usami S, et
al. (1997) Differential localization of delta glutamate receptors in the rat
cerebellum: coexpression with AMPA receptors in parallel fiber-spine synapses
and absence from climbing fiber-spine synapses. J Neurosci 17: 834–842.
11. Zhao HM, Wenthold RJ, Wang YX, Petralia RS (1997) Delta-glutamate
receptors are differentially distributed at parallel and climbing fiber synapses on
Purkinje cells. J Neurochem 68: 1041–1052.
12. Kashiwabuchi N, Ikeda K, Araki K, Hirano T, Shibuki K, et al. (1995)
Impairment of motor coordination, Purkinje cell synapse formation, and
cerebellar long-term depression in GluRd2 mutant mice. Cell 81: 245–252.
13. Kurihara H, Hashimoto K, Kano M, Takayama C, Sakimura K, et al. (1997)
Impaired parallel fiber–.Purkinje cell synapse stabilization during cerebellar
development of mutant mice lacking the glutamate receptor d2 subunit.
J Neurosci 17: 9613–9623.
14. Lalouette A, Guenet JL, Vriz S (1998) Hotfoot mouse mutations affect the d2
glutamate receptor gene and are allelic to lurcher. Genomics 50: 9–13.
15. Lalonde R, Bensoula AN, Filali M (1995) Rotarod sensorimotor learning in
cerebellar mutant mice. Neuroscience Research 22: 423–426.
16. Hirano T, Kasono K, Araki K, Mishina M (1995) Suppression of LTD in
cultured Purkinje cells deficient in the glutamate receptor d2 subunit.
Neuroreport 6: 524–526.
17. Zuo J, De Jager PL, Takahashi KA, Jiang W, Linden DJ, et al. (1997)
Neurodegeneration in Lurcher mice caused by mutation in d2 glutamate
receptor gene. Nature 388: 769–773.
18. Kohda K, Wang Y, Yuzaki M (2000) Mutation of a glutamate receptor motif
reveals its role in gating and d2 receptor channel properties. Nat Neurosci 3:
19. Wollmuth LP, Kuner T, Jatzke C, Seeburg PH, Heintz N, et al. (2000) The
Lurcher mutation identifies d2 as an AMPA/kainate receptor-like channel that is
potentiated by Ca(2+). J Neurosci 20: 5973–5980.
20. Yue Z, Horton A, Bravin M, DeJager PL, Selimi F, et al. (2002) A novel protein
complex linking the d2 glutamate receptor and autophagy: implications for
neurodegeneration in lurcher mice. Neuron 35: 921–933.
21. Levine B, Klionsky DJ (2004) Development by self-digestion: molecular
mechanisms and biological functions of autophagy. Dev Cell 6: 463–477.
22. Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, et al. (2006)
Suppression of basal autophagy in neural cells causes neurodegenerative disease
in mice. Nature 441: 885–889.
23. Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, et al. (2006) Loss of
autophagy in the central nervous system causes neurodegeneration in mice.
Nature 441: 880–884.
24. Cory S, Adams JM (2002) The Bcl2 family: regulators of the cellular life-or-
death switch. Nat Rev Cancer 2: 647–656.
25. Sharpe JC, Youle RJ (2004) Control of mitochondrial permeability by Bcl-2
family members. Biochim Biophys Acta 1644: 107–113.
26. Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, et al. (1996)
bcl-w, a novel member of the bcl-2 family, promotes cell survival. Oncogene 13:
27. Jiang X, Wang X (2004) Cytochrome C-mediated apoptosis. Annu Rev
Biochem 73: 87–106.
28. O’Reilly LA, Print C, Hausmann G, Moriishi K, Cory S, et al. (2001) Tissue
expression and subcellular localization of the pro-survival molecule Bcl-w. Cell
Death Differ 8: 486–494.
29. Hamner S, Skoglosa Y, Lindholm D (1999) Differential expression of bcl-w and
bcl-x messenger RNA in the developing and adult rat nervous system.
Neuroscience 91: 673–684.
30. Ross AJ, Waymire KG, Moss JE, Parlow AF, Skinner MK, et al. (1998)
Testicular degeneration in Bclw-deficient mice. Nature Genetics 18: 251–256.
31. Print CG, Loveland KL, Gibson L, Meehan T, Stylianou A, et al. (1998)
Apoptosis regulator bcl-w is essential for spermatogenesis but appears otherwise
redundant. Proc Natl Acad Sci U S A 95: 12424–12431.
32. Liang XH, Mungal S, Ayscue A, Meissner JD, Wodnicki P (1998) Protection
against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting
protein. J Virol 72: 8586–8596.
33. Pattingre S, Tassa A, Qu X, Garuti R, Liang XH, et al. (2005) Bcl-2
antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 122: 927–939.
34. Erlich S, Mizrachy L, Segev O, Lindenboim L, Zmira O, et al. (2007)
Differential interactions between Beclin 1 and Bcl-2 family members. Autophagy
35. Lalouette A, Lohof A, Sotelo C, Guenet J, Mariani J (2001) Neurobiological
effects of a null mutation depend on genetic context: comparison between two
hotfoot alleles of the d2 ionotropic glutamate receptor. Neuroscience 105:
36. Wang Y, Matsuda S, Drews V, Torashima T, Meisler MH, et al. (2003) A hot
spot for hotfoot mutations in the gene encoding the d2 glutamate receptor.
Eur J Neurosci 17: 1581–1590.
37. Palay SF, Chan-Palay V (1974) Cerebellar Cortex, Cytology and Organization.
New York: Springer.
38. Lalouette A, Lohof A, Sotelo C, Guenet J, Mariani J (2001) Neurobiological
effects of a null mutation depend on genetic context: comparison between two
hotfoot alleles of the delta-2 ionotropic glutamate receptor. Neuroscience 105:
39. Sango K, McDonald MP, Crawley JN, Mack ML, Tifft CJ, et al. (1996) Mice
lacking both subunits of lysosomal beta-hexosaminidase displays gangliosidosis
and mucopolysaccharidosis. Nat Genet 14: 348–352.
40. Berry P, Bradley H (1976) The growth of the dendritic trees of Purkinje cells in
the cerebellum of the rat. Brain Research 112: 1–35.
41. Luo L, Hensch TK, Ackerman L, Barbel S, Jan LY, Jan YN (1996) Differential
effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and
spines. Nature 379: 837–840.
42. Vecellio M, Schwaller B, Meyer M, Hunziker W, Celio MR (2000) Alterations in
Purkinje cell spines of calbindin D-28 k and parvalbumin knock-out mice.
Eur J Neurosci 12: 945–954.
43. Karbowski M, Lee YJ, Gaume B, Jeong SY, Frank S, et al. (2002) Spatial and
temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2
during apoptosis. J Cell Biol 159: 931–938.
44. Karbowski M, Arnoult D, Chen H, Chan DC, Smith CL, et al. (2004)
Quantitation of mitochondrial dynamics by photolabeling of individual
organelles shows that mitochondrial fusion is blocked during the Bax activation
phase of apoptosis. J Cell Biol 164: 493–499.
45. Karbowski M, Norris KL, Cleland MM, Jeong SY, Youle RJ (2006) Role of Bax
and Bak in mitochondrial morphogenesis. Nature 443: 658–662.
46. Jagasia R, Grote P, Westermann B, Conradt B (2005) DRP-1-mediated
mitochondrial fragmentation during EGL-1-induced cell death in C. elegans.
Nature 433: 754–760.
Bcl-w and Grid2 Control Dendrite Development
PLoS Genetics | www.plosgenetics.org12June 2008 | Volume 4 | Issue 6 | e1000097
47. Arnoult D, Rismanchi N, Grodet A, Roberts RG, Seeburg DP, et al. (2005)
Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated
mitochondrial fission and mitoptosis during programmed cell death. Curr Biol
48. Benard G, Bellance N, James D, Parrone, P, Fernandez H, et al. (2007)
Mitochondrial fission in apoptosis, neurodegeneration and aging. J Cell Sci
120(Pt 5): 838–848.
49. Sin WC, Haas K, Ruthazer ES, Cline HT (2002) Dendrite growth increased by
visual activity requires NMDA receptor and Rho GTPases. Nature 419: 475–80.
50. Hatten ME, Heintz N (1995) Mechanisms of neural patterning and specification
in the developing cerebellum. Annu Rev Neurosci 18: 385–408a.
51. Chen H, McCaffery JM, Chan DC (2007) Mitochondrial fusion protects against
neurodegeneration in the cerebellum. Cell 130: 548–562.
52. Sugioka R, Shimizu S, Tsujimoto Y (2004) Fzo1, a protein involved in
mitochondrial fusion, inhibits apoptosis. J Biol Chem 279: 52726–52734.
53. Olichon A, Baricault L, Gas N, Guillou E, Valette A, et al. (2003) Loss of OPA1
perturbates the mitochondrial inner membrane structure and integrity, leading
to cytochrome c release and apoptosis. J Biol Chem 278: 7743–7746.
54. McBride HM, Neuspiel M, Wasiak S (2006) Mitochondria: More than just a
powerhouse. Curr Biol 16: R551–560.
55. Jan YN, Jan LY (2003) The Control of Dendrite Development. Neuron 40:
56. Van Aelst L, Cline HT (2004) Rho GTPases and activity-dependent dendrite
development. Curr Opin Neurobiol 14: 297–304.
57. Chen Y, Bender RA, Brunson KL, Pomper JK, Grigoriadis DE, et al. (2004)
Modulation of dendritic differentiation by corticotropin-releasing factor in the
developing hippocampus. Proc Natl Acad Sci U S A 101: 15782–15787.
Bcl-w and Grid2 Control Dendrite Development
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