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Erythroid anion transporter assembly is mediated by a developmentally regulated recruitment onto a preassembled membrane cytoskeleton

Cox, John V. and Stack, Jeffrey H. and Lazarides, Elias (1987) Erythroid anion transporter assembly is mediated by a developmentally regulated recruitment onto a preassembled membrane cytoskeleton. Journal of Cell Biology, 105 (9). pp. 1405-1416. ISSN 0021-9525. PMCID PMC2114816. https://resolver.caltech.edu/CaltechAUTHORS:COXjcb87

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Abstract

Analysis of the expression and assembly of the anion transporter by metabolic pulse-chase and steady-state protein and RNA measurements reveals that the extent of association of band 3 with the membrane cytoskeleton varies during chicken embryonic development. Pulse-chase studies have indicated that band 3 polypeptides do not associate with the membrane cytoskeleton until they have been transported to the plasma membrane. At this time, band 3 polypeptides are slowly recruited, over a period of hours, onto a preassembled membrane cytoskeletal network and the extent of this cytoskeletal assembly is developmentally regulated. Only 3% of the band 3 polypeptides are cytoskeletal-associated in 4-d erythroid cells vs. 93% in 10-d erythroid cells and 36% in 15-d erythroid cells. This observed variation appears to be regulated primarily at the level of recruitment onto the membrane cytoskeleton rather than by different transport kinetics to the membrane or differential turnover of the soluble and insoluble polypeptides and is not dependent upon the lineage or stage of differentiation of the erythroid cells. Steady-state protein and RNA analyses indicate that the low levels of cytoskeletal band 3 very early in development most likely result from limiting amounts of ankyrin and protein 4.1, the membrane cytoskeletal binding sites for band 3. As embryonic development proceeds, ankyrin and protein 4.1 levels increase with a concurrent rise in the level of cytoskeletal band 3 until, on day 10 of development, virtually all of the band 3 polypeptides are cytoskeletal bound. After day 10, the levels of total and cytoskeletal band 3 decline, whereas ankyrin and protein 4.1 continue to accumulate until day 18, indicating that the cytoskeletal association of band 3 is not regulated solely by the availability of membrane cytoskeletal binding sites at later stages of development. Thus, multiple mechanisms appear to regulate the recruitment of band 3 onto the erythroid membrane cytoskeleton during chicken embryonic development.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1083/jcb.105.3.1405DOIArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/pmc2114816/PubMed CentralArticle
Additional Information:© 1987 by The Rockefeller University Press. RUP grants the public the non-exclusive right to copy, distribute, or display the Work under a Creative Commons Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ and http://creativecommons.org/licenses/by-nc-sa/3.0/legalcode. Received for publication 18 March 1987, and in revised form 20 May 1987. We thank Dr. John Ngai for providing the pSP6T7 construct of the adenosine phosphoribosyl transferase gene. This work was supported by grants from the National Institutes of Health (AG-06078A, HL-35801A) and National Science Foundation (DCB 8215658). Dr. Cox was supported by a postdoctoral fellowship from the American Heart Association, Greater Los Angeles Affiliate; and J. Stack was supported by a National Research Service Award (T32 GM-07616) from the National Institute of General Medical Sciences.
Funders:
Funding AgencyGrant Number
NIHAG-06078A
NIHHL-35801A
NSFDCB-8215658
American Heart Association, Greater Los Angeles AffiliateUNSPECIFIED
NIH Predoctoral FellowshipT32 GM-07616
Issue or Number:9
PubMed Central ID:PMC2114816
Record Number:CaltechAUTHORS:COXjcb87
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:COXjcb87
Usage Policy:RUP grants the public the non-exclusive right to copy, distribute, or display the Work under a Creative Commons Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ and http://creativecommons.org/licenses/by-nc-sa/3.0/legalcode.
ID Code:10705
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:04 Jun 2008
Last Modified:08 Jul 2020 17:15

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