PMID- 15062984
OWN - NLM
STAT- MEDLINE
DCOM- 20040720
LR  - 20101118
IS  - 0306-4522 (Print)
IS  - 0306-4522 (Linking)
VI  - 125
IP  - 2
DP  - 2004
TI  - Kinase- and rapsyn-independent activities of the muscle-specific kinase (MuSK).
PG  - 417-26
AB  - The muscle-specific receptor tyrosine kinase (MuSK) is co-localized with 
      nicotinic acetylcholine receptors (AChRs) in the postsynaptic membrane of the 
      skeletal neuromuscular junction, and is required for all known aspects of 
      postsynaptic differentiation. Studies in vitro have shown that Z(+)-agrin, a 
      nerve-derived proteoglycan, activates MuSK's kinase activity to promote 
      clustering of AChRs and MuSK itself with a cytoplasmic, receptor-associated 
      protein, rapsyn. These studies, however, have used soluble forms of agrin, 
      whereas agrin is cell- or matrix-attached in vivo. We show here that immobilized 
      (particle- or cell-attached) agrin but not soluble agrin is able to aggregate 
      MuSK in the absence of rapsyn and that this aggregation does not require MuSK's 
      kinase activity but does require MuSK's cytoplasmic domain. Moreover, immobilized 
      agrin can promote clustering of AChRs by a mechanism that requires MuSK and 
      rapsyn but does not require MuSK's kinase activity. These results imply that 
      rapsyn and signaling components activated by MuSK kinase may be dispensable for 
      some early aspects of postsynaptic differentiation.
FAU - Bromann, P A
AU  - Bromann PA
AD  - Department of Anatomy and Neurobiology, Washington University Medical School, 660 
      South Euclid, St. Louis, MO 63110, USA.
FAU - Zhou, H
AU  - Zhou H
FAU - Sanes, J R
AU  - Sanes JR
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Neuroscience
JT  - Neuroscience
JID - 7605074
RN  - 0 (Agrin)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Muscle Proteins)
RN  - 0 (Neural Cell Adhesion Molecules)
RN  - 0 (Receptors, Cholinergic)
RN  - 0 (Receptors, Nicotinic)
RN  - 0 (peripheral membrane protein 43K)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - EC 2.7.- (Phosphotransferases)
RN  - EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
RN  - EC 2.7.10.1 (MUSK protein, human)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Agrin/pharmacology/physiology
MH  - Animals
MH  - CHO Cells
MH  - Cells, Cultured
MH  - Cricetinae
MH  - Cricetulus
MH  - Embryo, Mammalian
MH  - Enzyme Activation
MH  - Green Fluorescent Proteins
MH  - Humans
MH  - Immunohistochemistry/methods
MH  - Luminescent Proteins/metabolism
MH  - Mice
MH  - Mice, Mutant Strains
MH  - Muscle Proteins/genetics/*metabolism
MH  - Myoblasts/drug effects/*metabolism
MH  - Neural Cell Adhesion Molecules/metabolism
MH  - Phosphatidylinositol 3-Kinases/metabolism
MH  - Phosphotransferases/*metabolism
MH  - Receptor Aggregation/drug effects/physiology
MH  - Receptor Protein-Tyrosine Kinases/*metabolism
MH  - Receptors, Cholinergic/*metabolism
MH  - Receptors, Nicotinic/metabolism
MH  - Signal Transduction
MH  - Transfection/methods
EDAT- 2004/04/06 05:00
MHDA- 2004/07/21 05:00
CRDT- 2004/04/06 05:00
PHST- 2003/12/15 00:00 [accepted]
PHST- 2004/04/06 05:00 [pubmed]
PHST- 2004/07/21 05:00 [medline]
PHST- 2004/04/06 05:00 [entrez]
AID - S0306452203009497 [pii]
AID - 10.1016/j.neuroscience.2003.12.031 [doi]
PST - ppublish
SO  - Neuroscience. 2004;125(2):417-26. doi: 10.1016/j.neuroscience.2003.12.031.