LASP1
LASP1 (LIM and SH3 protein 1, also known as MLN50 and Lasp-1) is a cytoskeletal protein that helps regulate dynamic, actin-based cellular activities. It belongs to the nebulin family of actin-binding proteins and carries both a LIM motif and an SH3 domain. Browse Assay Genie's current range of LASP1 research reagents below, or read on for the biology behind the target.
LASP1 plays an important role in the regulation of dynamic, actin-based cytoskeletal activities. It is described as a cAMP- and cGMP-dependent signalling protein that binds to the actin cytoskeleton at extensions of the cell membrane. UniProt annotates its location as the cell cortex and the cytoskeleton within the cytoplasm.
Agonist-dependent changes in LASP1 phosphorylation may also help regulate actin-associated ion transport activities. This has been proposed not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types, which links the protein to the control of specialised epithelial function as well as to general cytoskeletal dynamics.
The LASP1 gene encodes a member of a subfamily of LIM proteins, defined by a LIM motif together with a Src homology region 3 (SH3) domain. HGNC places it in the LIM domain containing, nebulin family and SH3 domain containing groups, and also lists it among the microRNA protein coding host genes. The mouse and rat orthologs are both named Lasp1. According to the NCBI Gene summary, the encoded protein has been linked to metastatic breast cancer, haematopoietic tumours such as B-cell lymphomas, and colorectal cancer, which has made LASP1 a protein of interest in cancer cell biology.
LASP1 helps regulate dynamic actin-based cytoskeletal activities and binds actin at extensions of the cell membrane.
LASP1 is a cAMP- and cGMP-dependent signalling protein, making it relevant to studies of cyclic nucleotide pathways.
LASP1 has been linked to metastatic breast cancer, B-cell lymphomas and colorectal cancer.
Agonist-dependent LASP1 phosphorylation may regulate actin-associated ion transport in parietal and other F-actin-rich secretory epithelial cells.
LASP1 plays an important role in regulating dynamic, actin-based cytoskeletal activities. It binds the actin cytoskeleton at extensions of the cell membrane and acts as a cAMP- and cGMP-dependent signalling protein. Its phosphorylation may also influence actin-associated ion transport in secretory epithelial cells.
The HGNC full name is LIM and SH3 protein 1, and UniProt calls the protein LIM and SH3 domain protein 1. Recorded aliases are MLN50 and Lasp-1. The names refer to its LIM motif and SH3 domain, and its place in the nebulin family of actin-binding proteins.
NCBI Gene reports that LASP1 has been linked to metastatic breast cancer, B-cell lymphomas and colorectal cancer. Orthologs named Lasp1 exist in mouse and rat, so rodent models can be used; check the datasheet of any product for its validated reactivity.
Other actin-binding proteins, LIM and SH3 domain proteins and cytoskeletal signalling targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q14847; product specifications from Assay Genie datasheets.