PMID- 19038220
OWN - NLM
STAT- MEDLINE
DCOM- 20090116
LR  - 20211020
IS  - 1097-4199 (Electronic)
IS  - 0896-6273 (Print)
IS  - 0896-6273 (Linking)
VI  - 60
IP  - 4
DP  - 2008 Nov 26
TI  - A mammalian homolog of Drosophila tumorous imaginal discs, Tid1, mediates agrin 
      signaling at the neuromuscular junction.
PG  - 625-41
LID - 10.1016/j.neuron.2008.09.025 [doi]
AB  - Motoneuron-derived agrin clusters nicotinic acetylcholine receptors (AChRs) in 
      mammalian muscle cells. We used two-hybrid screens to identify a protein, 
      tumorous imaginal discs (Tid1), that binds to the cytoplasmic domain of 
      muscle-specific kinase (MuSK), a major component of the agrin receptor. Like 
      MuSK, Tid1 colocalizes with AChRs at developing, adult, and denervated motor 
      endplates. Knockdown of Tid1 by short hairpin RNA (shRNA) in skeletal muscle 
      fibers dispersed synaptic AChR clusters and impaired neuromuscular transmission. 
      In cultured myotubes, Tid1 knockdown inhibited AChR clustering, as well as 
      agrin-induced activation of the Rac and Rho small GTPases and tyrosine 
      phosphorylation of the AChR, without affecting MuSK activation. Tid1 knockdown 
      also decreased Dok-7-induced clustering of AChRs. Overexpression of the 
      N-terminal half of Tid1 induced agrin- and MuSK-independent phosphorylation and 
      clustering of AChRs. These results demonstrate that Tid1 is an essential 
      component of the agrin signaling pathway, crucial for synaptic development.
FAU - Linnoila, Jenny
AU  - Linnoila J
AD  - Molecular Pharmacology Graduate Training Program, University of Pittsburgh School 
      of Medicine, Pittsburgh, PA 15261, USA. jenny.linnoila@gmail.com
FAU - Wang, Ying
AU  - Wang Y
FAU - Yao, Yun
AU  - Yao Y
FAU - Wang, Zuo-Zhong
AU  - Wang ZZ
LA  - eng
GR  - T32 GM008424/GM/NIGMS NIH HHS/United States
GR  - F30 NS053013-01A2/NS/NINDS NIH HHS/United States
GR  - R01 NS038301/NS/NINDS NIH HHS/United States
GR  - T32 GM08424/GM/NIGMS NIH HHS/United States
GR  - T32 GM008424-11/GM/NIGMS NIH HHS/United States
GR  - R01-NS038301/NS/NINDS NIH HHS/United States
GR  - R01 NS038301-09/NS/NINDS NIH HHS/United States
GR  - F30 NS053013/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Neuron
JT  - Neuron
JID - 8809320
RN  - 0 (Agrin)
RN  - 0 (Dnaja3 protein, mouse)
RN  - 0 (Dok-7 protein, mouse)
RN  - 0 (HSP40 Heat-Shock Proteins)
RN  - 0 (Muscle Proteins)
RN  - 0 (Receptors, Cholinergic)
RN  - EC 2.7.10.1 (MuSK protein, mouse)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
SB  - IM
CIN - Neuron. 2008 Nov 26;60(4):526-8. PMID: 19038209
MH  - Agrin/*metabolism
MH  - Animals
MH  - Cell Line
MH  - Down-Regulation/genetics
MH  - Drosophila/genetics/metabolism
MH  - GTP Phosphohydrolases/metabolism
MH  - HSP40 Heat-Shock Proteins/genetics/*metabolism
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Muscle Proteins/genetics/metabolism
MH  - Neuromuscular Junction/cytology/*embryology/growth & development
MH  - Organ Culture Techniques
MH  - Phosphorylation
MH  - Presynaptic Terminals/metabolism/ultrastructure
MH  - RNA Interference/physiology
MH  - Receptor Aggregation/*physiology
MH  - Receptor Protein-Tyrosine Kinases/*metabolism
MH  - Receptors, Cholinergic/*metabolism
MH  - Signal Transduction/physiology
PMC - PMC3225410
MID - NIHMS83124
EDAT- 2008/11/29 09:00
MHDA- 2009/01/17 09:00
PMCR- 2011/11/28
CRDT- 2008/11/29 09:00
PHST- 2007/07/09 00:00 [received]
PHST- 2008/05/14 00:00 [revised]
PHST- 2008/09/12 00:00 [accepted]
PHST- 2008/11/29 09:00 [pubmed]
PHST- 2009/01/17 09:00 [medline]
PHST- 2008/11/29 09:00 [entrez]
PHST- 2011/11/28 00:00 [pmc-release]
AID - S0896-6273(08)00799-X [pii]
AID - 10.1016/j.neuron.2008.09.025 [doi]
PST - ppublish
SO  - Neuron. 2008 Nov 26;60(4):625-41. doi: 10.1016/j.neuron.2008.09.025.