{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Moyer JD"],"funding":["NCRR NIH HHS","NHLBI NIH HHS"],"pagination":["2590-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2953891"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["116(14)"],"pubmed_abstract":["The short actin filaments in the red blood cell (RBC) membrane skeleton are capped at their pointed ends by tropomodulin 1 (Tmod1) and coated with tropomyosin (TM) along their length. Tmod1-TM control of actin filament length is hypothesized to regulate spectrin-actin lattice organization and membrane stability. We used a Tmod1 knockout mouse to investigate the in vivo role of Tmod1 in the RBC membrane skeleton. Western blots of Tmod1-null RBCs confirm the absence of Tmod1 and show the presence of Tmod3, which is normally not present in RBCs. Tmod3 is present at only one-fifth levels of Tmod1 present on wild-type membranes, but levels of actin, TMs, adducins, and other membrane skeleton proteins remain unchanged. Electron microscopy shows that actin filament lengths are more variable with "],"journal":["Blood"],"pubmed_title":["Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton."],"pmcid":["PMC2953891"],"funding_grant_id":["R01 HL083464","R21 HL092535","P01 HL059561","HL092535","RR17573","P41 RR017573","HL083464","HL56949","R01 HL088468","HL088468","P01 HL056949","HL59561"],"pubmed_authors":["Kuypers FA","Fowler VM","Hartwig J","Nowak RB","Peters LL","Moyer JD","Kim NE","Larkin SK"],"additional_accession":[]},"is_claimable":false,"name":"Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton.","description":"The short actin filaments in the red blood cell (RBC) membrane skeleton are capped at their pointed ends by tropomodulin 1 (Tmod1) and coated with tropomyosin (TM) along their length. Tmod1-TM control of actin filament length is hypothesized to regulate spectrin-actin lattice organization and membrane stability. We used a Tmod1 knockout mouse to investigate the in vivo role of Tmod1 in the RBC membrane skeleton. Western blots of Tmod1-null RBCs confirm the absence of Tmod1 and show the presence of Tmod3, which is normally not present in RBCs. Tmod3 is present at only one-fifth levels of Tmod1 present on wild-type membranes, but levels of actin, TMs, adducins, and other membrane skeleton proteins remain unchanged. Electron microscopy shows that actin filament lengths are more variable with ","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Oct","modification":"2025-05-31T22:57:06.44Z","creation":"2025-05-31T22:57:06.44Z"},"accession":"S-EPMC2953891","cross_references":{"pubmed":["20585041"],"doi":["10.1182/blood-2010-02-268458"]}}