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The Journal of Neuroscience, August 15, 2000, 20(16):6055-6062

Integrin ₁₁-Mediated Activation of Cyclin-Dependent Kinase 5 Activity Is Involved in Neurite Outgrowth and Human Neurofilament Protein H Lys-Ser-Pro Tail Domain Phosphorylation

Bing-Sheng Li¹, Lei Zhang², Jianguo Gu³, Niranjana D. Amin¹, and Harish C. Pant¹

¹ Laboratory of Neurochemistry, National Institute of Neurological Diseases and Stroke, ² Behavioral and Endocrinology Branch, National Institute of Mental Health, and ³ Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892-4130

Cellular adhesion to the extracellular matrix is mediated by a diverse class of / heterodimeric receptors known as integrins, which transduce signals to activate multiple intracellular signal transduction pathways within the cells. The signaling pathway linking integrins to mediate neuronal process outgrowth is not well understood. Here, we have provided evidence that intracellular signaling by the ₁₁ integrin-induced activation of cyclin-dependent kinase 5 (cdk5) is involved in neurite outgrowth and human neurofilament protein H (hNF-H) Lys-Ser-Pro (KSP) tail domain phosphorylation in differentiated human SH-SY5Y cells. The integrin ₁ and ₁ monoclonal antibodies and BL-1, a specific cdk5 inhibitor, inhibited these effects. We also demonstrated that cdk5 activity and hNF-H KSP tail domain phosphorylation were increased in cdk5/p35 and hNF-H tail domain co-transfected HEK293 cells grown on laminin. This increased hNF-H tail domain phosphorylation was triggered by cdk5 activation. Taken together, these results indicated that cdk5 may play an important role in promoting neurite outgrowth and hNF-H tail KSP domain phosphorylation through the integrin ₁₁ signaling pathway.

Key words: cdk5; p35; neurofilament; integrin; matrix; laminin; retinoic acid

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Copyright © 2000 Society for Neuroscience  0270-6474/00/20166055-08$05.00/0

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