Navigation Links
Laminin builds the neuromuscular synapse

Like a plug and a socket, a nerve and a muscle fiber mesh at the neuromuscular junction. New work by Nishimune et al published in the Journal of Cell Biology reveals that an extracellular matrix protein called laminin shapes both sides of the junction to ensure they fit together type="rel"doi="10.1083/jcb.2008.

A neuromuscular junction, or synapse, in a newborn mouse is functional but simple, with a globular nerve terminal meeting a flat, oval structure on the muscle fiber. As the animal matures, the nerve terminal branches into a claw shape, and the muscle side contorts into a matching conformation. But what coordinates these changes so the two sides mirror each other? The researchers think that one molecule in the synapse sculpts both sides.

Their chief suspect was the synapse-spanning protein laminin. Made by muscle and forming part of the sheath that covers muscle, the laminin protein has different domains called alpha, beta, and gamma chains. Previous work had shown that the beta2 chain of laminin spurs differentiation of the nerve terminal. The team has now found evidence that the alpha chains of laminin influence post-synaptic patterning. For example, maturation of the muscle side slowed in mice lacking the alpha5 chain of laminin in their muscles.

The researchers discovered that cell surface receptor molecules that recognize and bind laminin, are corralled by laminin on the muscle side of the synapse. These receptors, in turn, gather other receptors that respond to signals from the nerve. Overall, the work suggests that the beta and alpha chains of laminin together influence pre-synaptic and post-synaptic development, thus providing a way to coordinate maturation of the sending and receiving sides of the synapse.


Contact: Sati Motieram
Rockefeller University Press

Page: 1

Related biology news :

1. GM, Coskata partnership builds on Oklahoma State University biofuels research
2. New approach builds better proteins inside a computer
3. A key enzyme helps keep the synapse on track
4. Breakthrough technology observes synapse in real time, supporting theory of vesicular recycling
Post Your Comments:
(Date:5/6/2017)... 5, 2017 RAM Group , ... new breakthrough in biometric authentication based on a ... properties to perform biometric authentication. These new sensors are ... created by Ram Group and its partners. This sensor ... supply chains and security. Ram Group is a ...
(Date:4/17/2017)... NXT-ID, Inc. (NASDAQ: NXTD ) ("NXT-ID" or the "Company"), ... Report on Form 10-K on Thursday April 13, 2017 with the ... The ... section of the Company,s website at  under "SEC Filings," ... 2016 Year Highlights: Acquisition of ...
(Date:4/11/2017)... DUBLIN , Apr. 11, 2017 Research ... Tracking Market 2017-2021" report to their offering. ... The global eye tracking market to grow at ... The report, Global Eye Tracking Market 2017-2021, has been prepared based ... report covers the market landscape and its growth prospects over the ...
Breaking Biology News(10 mins):
(Date:10/10/2017)... ... 2017 , ... Dr. Bob Harman, founder and CEO of VetStem Biopharma, ... The event entitled “Stem Cells and Their Regenerative Powers,” was held on ... DVM, MPVM was joined by two human doctors: Peter B. Hanson, M.D., Chief of ...
(Date:10/10/2017)... ... October 10, 2017 , ... The ... prestigious awards honoring scientists who have made outstanding contributions to analytical ... during Pittcon 2018, the world’s leading conference and exposition for laboratory science, which ...
(Date:10/9/2017)... ... October 09, 2017 , ... The Giving Tree Wellness Center ... the needs of consumers who are incorporating medical marijuana into their wellness and ... , As operators of two successful Valley dispensaries, The Giving Tree’s two founders, ...
(Date:10/7/2017)...  The 2017 Nobel Prize in Chemistry recognizes ... Joachim Frank and Richard Henderson ... (cryo-EM) have helped to broaden the use ... The winners worked with systems manufactured by Thermo ... resolved, three-dimensional images of protein structures that lead ...
Breaking Biology Technology: