Myo3A, one of two class III myosin genes expressed in vertebrate retina, is localized to the calycal processes of rod and cone photoreceptors and is expressed in the sacculus

被引:53
作者
Dosé, AC [1 ]
Hillman, DW
Wong, C
Sohlberg, L
Lin-Jones, J
Burnside, B
机构
[1] Univ Calif Berkeley, Berkeley, CA 94720 USA
[2] Ingenu Inc, Mountain View, CA 94043 USA
[3] Univ Pacific, Sch Pharm, Stockton, CA 95211 USA
[4] Bayer Pharmaceut Div, Berkeley, CA 94701 USA
关键词
D O I
10.1091/mbc.E02-06-0317
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The striped bass has two retina-expressed class III myosin genes, each composed of a kinase, motor, and tail domain. We report the cloning, sequence analysis, and expression patterns of the long (Myo3A) and short (Myo3B) class III myosins, as well as cellular localization and biochemical characterization of the long isoform, Myo3A. Myo3A (209 kDa) is expressed in the retina, brain, testis, and sacculus, and Myo3B (155 kDa) is expressed in the retina, intestine, and testis. The tails of these two isoforms contain two highly conserved domains, 3THDI and 3THDII. Whereas Myo3B has three IQ motifs, Myo3A has nine IQ motifs, four in its neck and five in its tail domain. Myo3A localizes to actin filament bundles of photoreceptors and is concentrated in the calycal processes. An anti-Myo3A antibody decorates the actin cytoskeleton of rod inner/outer segments, and this labeling is reduced by the presence of ATP. The ATP-sensitive actin association is a feature characteristic of myosin motors. The numerous IQ motifs may play a structural or signaling role in the Myo3A, and its localization to calycal processes indicates that this myosin mediates a local function at this site in vertebrate photoreceptors.
引用
收藏
页码:1058 / 1073
页数:16
相关论文
共 77 条
[1]   VITRONECTIN RECEPTOR EXPRESSION AND DISTRIBUTION AT THE PHOTORECEPTOR-RETINAL PIGMENT EPITHELIAL INTERFACE [J].
ANDERSON, DH ;
JOHNSON, LV ;
HAGEMAN, GS .
JOURNAL OF COMPARATIVE NEUROLOGY, 1995, 360 (01) :1-16
[2]   InterPro - an integrated documentation resource for protein families, domains and functional sites [J].
Apweiler, R ;
Attwood, TK ;
Bairoch, A ;
Bateman, A ;
Birney, E ;
Biswas, M ;
Bucher, P ;
Cerutti, L ;
Corpet, F ;
Croning, MDR ;
Durbin, R ;
Falquet, L ;
Fleischmann, W ;
Gouzy, J ;
Hermjakob, H ;
Hulo, N ;
Jonassen, I ;
Kahn, D ;
Kanapin, A ;
Karavidopoulou, Y ;
Lopez, R ;
Marx, B ;
Mulder, NJ ;
Oinn, TM ;
Pagni, M ;
Servant, F ;
Sigrist, CJA ;
Zdobnov, EM .
BIOINFORMATICS, 2000, 16 (12) :1145-1150
[3]   ALPHA-ACTININ AND ACTIN IN THE OUTER RETINA - A DOUBLE IMMUNOELECTRON MICROSCOPIC STUDY [J].
ARIKAWA, K ;
WILLIAMS, DS .
CELL MOTILITY AND THE CYTOSKELETON, 1991, 18 (01) :15-25
[4]   PEST SEQUENCES IN CALMODULIN-BINDING PROTEINS [J].
BARNES, JA ;
GOMES, AV .
MOLECULAR AND CELLULAR BIOCHEMISTRY, 1995, 149 :17-27
[5]   Regulation of the enzymatic and motor activities of myosin I [J].
Barylko, B ;
Binns, DD ;
Albanesi, JP .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2000, 1496 (01) :23-35
[6]  
Battelle BA, 1998, J NEUROSCI, V18, P4548
[7]   TEDS RULE - A MOLECULAR RATIONALE FOR DIFFERENTIAL REGULATION OF MYOSINS BY PHOSPHORYLATION OF THE HEAVY-CHAIN HEAD [J].
BEMENT, WM ;
MOOSEKER, MS .
CELL MOTILITY AND THE CYTOSKELETON, 1995, 31 (02) :87-92
[8]   IDENTIFICATION AND OVERLAPPING EXPRESSION OF MULTIPLE UNCONVENTIONAL MYOSIN GENES IN VERTEBRATE CELL-TYPES [J].
BEMENT, WM ;
HASSON, T ;
WIRTH, JA ;
CHENEY, RE ;
MOOSEKER, MS .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (14) :6549-6553
[9]   A millennial myosin census [J].
Berg, JS ;
Powell, BC ;
Cheney, RE .
MOLECULAR BIOLOGY OF THE CELL, 2001, 12 (04) :780-794
[10]  
BERS DM, 1994, METHOD CELL BIOL, V40, P3