<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>143(5)</volume><submitter>Gregory SL</submitter><pubmed_abstract>Mutations in kakapo were recovered in genetic screens designed to isolate genes required for integrin-mediated adhesion in Drosophila. We cloned the gene and found that it encodes a large protein (>5,000 amino acids) that is highly similar to plectin and BPAG1 over the first 1,000-amino acid region, and contains within this region an alpha-actinin type actin-binding domain. A central region containing dystrophin-like repeats is followed by a carboxy domain that is distinct from plectin and dystrophin, having neither the intermediate filament-binding domain of plectin nor the dystroglycan/syntrophin-binding domain of dystrophin. Instead, Kakapo has a carboxy terminus similar to the growth arrest-specific protein Gas2. Kakapo is strongly expressed late during embryogenesis at the most promin</pubmed_abstract><journal>The Journal of cell biology</journal><pagination>1271-82</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2133084</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>kakapo, a gene required for adhesion between and within cell layers in Drosophila, encodes a large cytoskeletal linker protein related to plectin and dystrophin.</pubmed_title><pmcid>PMC2133084</pmcid><pubmed_authors>Gregory SL</pubmed_authors><pubmed_authors>Brown NH</pubmed_authors></additional><is_claimable>false</is_claimable><name>kakapo, a gene required for adhesion between and within cell layers in Drosophila, encodes a large cytoskeletal linker protein related to plectin and dystrophin.</name><description>Mutations in kakapo were recovered in genetic screens designed to isolate genes required for integrin-mediated adhesion in Drosophila. We cloned the gene and found that it encodes a large protein (>5,000 amino acids) that is highly similar to plectin and BPAG1 over the first 1,000-amino acid region, and contains within this region an alpha-actinin type actin-binding domain. A central region containing dystrophin-like repeats is followed by a carboxy domain that is distinct from plectin and dystrophin, having neither the intermediate filament-binding domain of plectin nor the dystroglycan/syntrophin-binding domain of dystrophin. Instead, Kakapo has a carboxy terminus similar to the growth arrest-specific protein Gas2. Kakapo is strongly expressed late during embryogenesis at the most promin</description><dates><release>1998-01-01T00:00:00Z</release><publication>1998 Nov</publication><modification>2025-04-05T08:52:34.015Z</modification><creation>2019-03-26T23:02:30Z</creation></dates><accession>S-EPMC2133084</accession><cross_references><pubmed>9832555</pubmed><doi>10.1083/jcb.143.5.1271</doi></cross_references></HashMap>