- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Moore, K. J.
- Articles by Jenkins, N. A.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Moore, K. J.
- Articles by Jenkins, N. A.
Genetics, Vol 119, 933-941, Copyright © 1988
INVESTIGATIONS |
The Murine Dilute Suppressor Gene dsu Suppresses the Coat-Color Phenotype of Three Pigment Mutations That Alter Melanocyte Morphology, d, ash and ln
K. J. Moore, D. A. Swing, E. M. Rinchik, M. L. Mucenski, A. M. Buchberg, N. G. Copeland and N. A. Jenkins
Mammalian Genetics Laboratory, Bionetics Research, Inc., Basic Research Program, National Cancer Institute-Frederick Cancer Research Facility, Frederick, Maryland 21701
The murine dilute suppressor gene, dsu, was identified because of its ability to suppress the dilute coat color of mice homozygous for the retrovirally induced allele (d(v)) of the dilute locus (d). dsu is unlinked to the d locus and has recently been shown to be semidominantly inherited. The dilute phenotype of d/d mice is the consequence of abnormal melanocyte morphology. While wild-type melanocytes are dendritic, d/d melanocytes are adendritic. dsu apparently suppresses the dilute phenotype by restoring normal melanocyte morphology. In addition to d, two other loci, ashen (ash) and leaden (ln), have been identified that produce a diluted coat color associated with adendritic melanocytes. Interestingly, d and ash are closely linked on chromosome 9 while dsu and ln are located on chromosome 1. In experiments described here, we present genetic mapping data between ash and d indicating that, despite their identical phenotypes, they are separate genes and are not intragenic complementing alleles of the same locus. We also show that dsu is only loosely linked to ln (approximately 9 cM proximal) and that dsu can suppress, at least partially, the coat color of ln/ln mice and ash/ash mice. The partial suppression of ln and ash coat colors is associated with the partial restoration of normal melanocyte morphology. These studies provide new insights into the mechanism of action of dsu and into the interrelationships between members of a family of pigment genes.
This article has been cited by other articles:
![]() |
B. L. Grosshans, D. Ortiz, and P. Novick Rabs and their effectors: Achieving specificity in membrane traffic PNAS, August 8, 2006; 103(32): 11821 - 11827. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. N. O'Sullivan, X. S. Wu, R. A. Rachel, J.-D. Huang, D. A. Swing, L. E. Matesic, J. A. Hammer III, N. G. Copeland, and N. A. Jenkins dsu functions in a MYO5A-independent pathway to suppress the coat color of dilute mice PNAS, November 30, 2004; 101(48): 16831 - 16836. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Strom, A. N. Hume, A. K. Tarafder, E. Barkagianni, and M. C. Seabra A Family of Rab27-binding Proteins. MELANOPHILIN LINKS Rab27a AND MYOSIN Va FUNCTION IN MELANOSOME TRANSPORT J. Biol. Chem., July 5, 2002; 277(28): 25423 - 25430. [Abstract] [Full Text] [PDF] |
||||
![]() |
X. Wu, F. Wang, K. Rao, J. R. Sellers, and J. A. Hammer III Rab27a Is an Essential Component of Melanosome Receptor for Myosin Va Mol. Biol. Cell, May 1, 2002; 13(5): 1735 - 1749. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. E. Matesic, R. Yip, A. E. Reuss, D. A. Swing, T. N. O'Sullivan, C. F. Fletcher, N. G. Copeland, and N. A. Jenkins Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice PNAS, August 10, 2001; (2001) 181336698. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. N. Hume, L. M. Collinson, A. Rapak, A. Q. Gomes, C. R. Hopkins, and M. C. Seabra Rab27a Regulates the Peripheral Distribution of Melanosomes in Melanocytes J. Cell Biol., February 20, 2001; 152(4): 795 - 808. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Bahadoran, E. Aberdam, F. Mantoux, R. Busca, K. Bille, N. Yalman, G. de Saint-Basile, R. Casaroli-Marano, J.-P. Ortonne, and R. Ballotti Rab27a: A Key to Melanosome Transport in Human Melanocytes J. Cell Biol., February 20, 2001; 152(4): 843 - 850. [Abstract] [Full Text] [PDF] |
||||
![]() |
X Wu, K Rao, M. Bowers, N. Copeland, N. Jenkins, and J. Hammer Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle J. Cell Sci., January 3, 2001; 114(6): 1091 - 1100. [Abstract] [PDF] |
||||
![]() |
S. M. Wilson, R. Yip, D. A. Swing, T. N. O'Sullivan, Y. Zhang, E. K. Novak, R. T. Swank, L. B. Russell, N. G. Copeland, and N. A. Jenkins A mutation in Rab27a causes the vesicle transport defects observed in ashen mice PNAS, June 14, 2000; (2000) 140212797. [Abstract] [Full Text] |
||||
![]() |
D. W. Provance Jr., M. Wei, V. Ipe, and J. A. Mercer Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution PNAS, December 10, 1996; 93(25): 14554 - 14558. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. M. Wilson, R. Yip, D. A. Swing, T. N. O'Sullivan, Y. Zhang, E. K. Novak, R. T. Swank, L. B. Russell, N. G. Copeland, and N. A. Jenkins A mutation in Rab27a causes the vesicle transport defects observed in ashen mice PNAS, July 5, 2000; 97(14): 7933 - 7938. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. E. Matesic, R. Yip, A. E. Reuss, D. A. Swing, T. N. O'Sullivan, C. F. Fletcher, N. G. Copeland, and N. A. Jenkins Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice PNAS, August 28, 2001; 98(18): 10238 - 10243. [Abstract] [Full Text] [PDF] |
||||




