Assembly of body wall muscle and muscle cell attachment structures in Caenorhabditis elegans
نویسندگان
چکیده
C. Elegans has four muscle quadrants that are used for locomotion. Contraction is converted to locomotion because muscle cells are anchored to the cuticle (the outer covering of the worm) by a specialized basement membrane and hemidesmosome structures in the hypodermis (a cellular syncytium that covers the worm and secretes the cuticle). To study muscle assembly, we have used antibodies to determine the spatial and temporal distribution of muscle and attachment structure components in wild-type and mutant C. elegans embryos. Myofibrillar components are first observed diffusely distributed in the muscle cells, and are expressed in some dividing cells. Later, the components accumulate at the membrane adjacent to the hypodermis where the sarcomeres will form, showing that the cells have become polarized. Assembly of muscle attachment structures is spatially and temporally coordinated with muscle assembly suggesting that important developmental signals may be passed between muscle and hypodermal cells. Analysis of embryos homozygous for mutations that affect muscle assembly show that muscle components closer to the membrane than the affected protein assemble quite well, while those further from the membrane do not. Our results suggest a model where lattice assembly is initiated at the membrane and the spatial organization of the structural elements of the muscle is dictated by membrane proximal events, not by the filament components themselves.
منابع مشابه
The LIM domain protein UNC-95 is required for the assembly of muscle attachment structures and is regulated by the RING finger protein RNF-5 in C. elegans
Here, we describe a new muscle LIM domain protein, UNC-95, and identify it as a novel target for the RING finger protein RNF-5 in the Caenorhabditis elegans body wall muscle. unc-95(su33) animals have disorganized muscle actin and myosin-containing filaments as a result of a failure to assemble normal muscle adhesion structures. UNC-95 is active downstream of PAT-3/beta-integrin in the assembly...
متن کاملMuscle cell attachment in Caenorhabditis elegans
In the nematode Caenorhabditis elegans, the body wall muscles exert their force on the cuticle to generate locomotion. Interposed between the muscle cells and the cuticle are a basement membrane and a thin hypodermal cell. The latter contains bundles of filaments attached to dense plaques in the hypodermal cell membranes, which together we have called a fibrous organelle. In an effort to define...
متن کاملDevelopment, structure, and maintenance of C. elegans body wall muscle.
In C. elegans, mutants that are defective in muscle function and/or structure are easy to detect and analyze since: 1) body wall muscle is essential for locomotion, and 2) muscle structure can be assessed by multiple methods including polarized light, electron microscopy (EM), Green Fluorescent Protein (GFP) tagged proteins, and immunofluorescence microscopy. The overall structure of the sarcom...
متن کاملThe Caenorhabditis elegans paxillin orthologue, PXL-1, is required for pharyngeal muscle contraction and for viability
We have identified the gene C28H8.6 (pxl-1) as the Caenorhabditis elegans orthologue of vertebrate paxillin. PXL-1 contains the four C-terminal LIM domains conserved in paxillin across all species and three of the five LD motifs found in the N-terminal half of most paxillins. In body wall muscle, PXL-1 antibodies and a full-length green fluorescent protein translational fusion localize to adhes...
متن کاملA Conserved LIM Protein That Affects Muscular Adherens Junction Integrity and Mechanosensory Function in Caenorhabditis elegans
We describe here the molecular and functional characterization of the Caenorhabditis elegans unc-97 gene, whose gene product constitutes a novel component of muscular adherens junctions. UNC-97 and homologues from several other species define the PINCH family, a family of LIM proteins whose modular composition of five LIM domains implicates them as potential adapter molecules. unc-97 expression...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of Cell Biology
دوره 124 شماره
صفحات -
تاریخ انتشار 1994