B-Crystallin phosphorylated at Ser-59 is localized in centrosomes and midbodies during mitosis
Authors: Inaguma Y.1; Ito H.1; Iwamoto I.1; Saga S.2; Kato K.1
Source: European Journal of Cell Biology, Volume 80, Number 12, December 2001 , pp. 741-748(8)
Publisher: Urban & Fischer
Abstract:
We have reported that the three serine residues in
B-crystallin are phosphorylated under various stress conditions. We prepared affinity-purified antibodies recognizing each of the phosphorylated serine residues (Ser-19, Ser-45, and Ser-59, respectively) in
B-crystallin with peptides (p19S, p45S, or p59S) that contained the corresponding phosphorylated serine residue. Immunocytochemically anti-p45S antibodies stained the cytoplasm of mitotic cells (J. Biol. Chem. 273, 28 346 28 354). We have now found that the anti-p59S antibodies recognize centrosomes and midbodies of dividing cells.
B-Crystallin was the only protein recognized by the anti-p59S antibodies in Western blot analyses of isolated centrosome fractions.
B-Crystallin phosphorylated at Ser-59 was localized at the microtubule organizing centers by means of double staining with anti-
-tubulin antibody in aster formation analysis and was co-localized with
-tubulin in centrosomes.
-Tubulin was co-immunoprecipitated with
B-crystallin in U373 glioma cell extracts. On the other hand, the location of the phosphorylated
B-crystallin deviated from that of
-tubulin or
-tubulin in the midbody region. Taken together with the evidences that several chaperones are distributed to centrosomes, these results suggest that
B-crystallin as a chaperone might be also involved in the quality control of proteins.
Keywords:
B-crystallin;
centrosomes;
midbodies
Language: English
Document Type: Original article
DOI: 10.1078/0171-9335-00203
Affiliations: 1: Department of Biochemistry, Institute for Developmental Research, Aichi Human Service Center, Aichi/Japan 2: Department of Pathology, Aichi Medical University, Aichi/Japan

Click here for Page Help