Work

Ubiquitination of red blood cell α‐spectrin does not affect heterodimer formation

Year: 2005

Type: article

Abstract: Erythrocyte alpha-spectrin is ubiquitinated in repeats alpha20/alpha21, which also represents the nucleation site for contact with the beta subunit which leads to heterodimer formation by a zippering mechanism. In this study we have determined the second-order rate constant for association of ubiquitinated alpha'-spectrin, nonubiquitinated alpha-spectrin, and beta-spectrin into the alpha'beta or alphabeta heterodimer. The rate constant for incorporation of monomers into heterodimers at 37 degrees C were (5.181 +/- 0.001) x 10(5) M(-1) sec(-1) for total alpha-spectrin (alpha + alpha'), (5.121 +/- 0.001) x 10(5) M(-1) sec(-1) for alpha'-spectrin, and (5.178 +/- 0.003) x 10(5) M(-1) sec(-1) for beta-spectrin. We conclude that ubiquitination of alpha-spectrin does not regulate heterodimer formation.

Source: American Journal of Hematology

DOI: 10.1002/ajh.20282

Authors: Mahnoush H. Riahi, David G. Kakhniashvili, Steven R. Goodman

Institutions: The University of Texas at Dallas, The University of Texas Southwestern Medical Center

Language: English

Topic: Erythrocyte Function and Pathophysiology

Subfield: Physiology (medical)

Field: Medicine

Domain: Health Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Heart, Lung, and Blood Institute

Awards: G4215687869, Southwestern Comprehensive Sickle Cell Center