PMID- 25376491
OWN - NLM
STAT- MEDLINE
DCOM- 20150701
LR  - 20191210
IS  - 1937-6448 (Print)
IS  - 1937-6448 (Linking)
VI  - 313
DP  - 2014
TI  - The UNC-45 myosin chaperone: from worms to flies to vertebrates.
PG  - 103-44
LID - B978-0-12-800177-6.00004-9 [pii]
LID - 10.1016/B978-0-12-800177-6.00004-9 [doi]
AB  - UNC-45 (uncoordinated mutant number 45) is a UCS (UNC-45, CRO1, She4p) domain 
      protein that is critical for myosin stability and function. It likely aides in 
      folding myosin during cellular differentiation and maintenance, and protects 
      myosin from denaturation during stress. Invertebrates have a single unc-45 gene 
      that is expressed in both muscle and nonmuscle tissues. Vertebrates possess one 
      gene expressed in striated muscle (unc-45b) and another that is more generally 
      expressed (unc-45a). Structurally, UNC-45 is composed of a series of alpha-helices 
      connected by loops. It has an N-terminal tetratricopeptide repeat domain that 
      binds to Hsp90 and a central domain composed of armadillo repeats. Its C-terminal 
      UCS domain, which is also comprised of helical armadillo repeats, interacts with 
      myosin. In this chapter, we present biochemical, structural, and genetic analyses 
      of UNC-45 in Caenorhabditis elegans, Drosophila melanogaster, and various 
      vertebrates. Further, we provide insights into UNC-45 functions, its potential 
      mechanism of action, and its roles in human disease.
FAU - Lee, Chi F
AU  - Lee CF
AD  - Department of Biology, San Diego State University, San Diego, CA, USA.
FAU - Melkani, Girish C
AU  - Melkani GC
AD  - Department of Biology, San Diego State University, San Diego, CA, USA.
FAU - Bernstein, Sanford I
AU  - Bernstein SI
AD  - Department of Biology, San Diego State University, San Diego, CA, USA.
LA  - eng
GR  - R01 AR055958/AR/NIAMS NIH HHS/United States
GR  - 5R01AR055958/AR/NIAMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Review
PL  - Netherlands
TA  - Int Rev Cell Mol Biol
JT  - International review of cell and molecular biology
JID - 101475846
RN  - 0 (Caenorhabditis elegans Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Muscle Proteins)
RN  - 0 (UNC-45 protein, Drosophila)
RN  - 0 (Unc45 protein, mouse)
RN  - 0 (Unc45b protein, zebrafish)
RN  - 0 (Xenopus Proteins)
RN  - 0 (Zebrafish Proteins)
RN  - 0 (unc-45 protein, C elegans)
RN  - EC 3.6.4.1 (Myosins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Caenorhabditis elegans/genetics/*metabolism
MH  - Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism
MH  - Crystallography, X-Ray
MH  - Drosophila Proteins/chemistry/genetics/metabolism
MH  - Drosophila melanogaster/genetics/*metabolism
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins/chemistry/genetics/metabolism
MH  - Mice
MH  - Models, Molecular
MH  - Molecular Chaperones/chemistry/genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Muscle Proteins
MH  - Mutation
MH  - Myosins/*metabolism
MH  - Protein Conformation
MH  - Protein Interaction Domains and Motifs
MH  - Structure-Activity Relationship
MH  - Xenopus/genetics/metabolism
MH  - Xenopus Proteins/genetics/metabolism
MH  - Zebrafish/genetics/metabolism
MH  - Zebrafish Proteins/chemistry/genetics/metabolism
PMC - PMC4225561
MID - NIHMS632140
OTO - NOTNLM
OT  - Chaperone
OT  - Hsp90
OT  - Muscle
OT  - Myosin
OT  - TPR domain
OT  - UCS protein
OT  - UNC-45
EDAT- 2014/11/08 06:00
MHDA- 2015/07/02 06:00
PMCR- 2015/01/01
CRDT- 2014/11/08 06:00
PHST- 2014/11/08 06:00 [entrez]
PHST- 2014/11/08 06:00 [pubmed]
PHST- 2015/07/02 06:00 [medline]
PHST- 2015/01/01 00:00 [pmc-release]
AID - B978-0-12-800177-6.00004-9 [pii]
AID - 10.1016/B978-0-12-800177-6.00004-9 [doi]
PST - ppublish
SO  - Int Rev Cell Mol Biol. 2014;313:103-44. doi: 10.1016/B978-0-12-800177-6.00004-9.